entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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|---|---|---|---|---|
Q9ZCS2
|
RS5_RICPR
|
Small ribosomal subunit protein uS5 (30S ribosomal protein S5)
|
MSKVKKNEEALSEVLVDVNRVTKVVKGGRRFAFSAYVVVGDKAGRVGAGHGKAKEVNEARGKAKQAAKKRMMKVPLYQNRTIHHDVVGKSGAAKVILRRAKAGTGVIAGGSMRAIFDSLGVHDIVAKSIGSTNVYAMISATFDALNKLASPKSIAIRRDKKVHEISIKSYIQVNE
|
With S4 and S12 plays an important role in translational accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}. Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. {ECO:0000255|HAMAP-Rule:MF_01307}.
|
Q9ZCS4
|
RL15_RICPR
|
Large ribosomal subunit protein uL15 (50S ribosomal protein L15)
|
MKLNELYNNLGAKKNKKRIARGIGSGKGKTAGRGIKGQKSRSGVAIKGFEGGQTPMIKRLPKRGFKCISTKKYNIINIYNIEEALTDGRLSTNDIITKEKLLEVGLINNKNLVKLLSICSDDFASPLSLKLDAYSSKAKYLIEKVGGQLL
|
Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01341}.
|
Q9ZCS5
|
SECY_RICPR
|
Protein translocase subunit SecY
|
MGQNFSKKSSNDLVNRIIFTLFMLIICRFGSFIPIPGIDSIALNSVAEKNQFGILGMFNMLSGGSLGRMSIFALAIMPYITASIIIQLMSVAYKPLENLKKEGETGKRKINQLSRYLTVLLASFQAYGVALSLESMVTNTGPVVILAGFFFRVTTVITLVVGTILLMWLGEQITQRGIGNGTSLIIFIGIISGVPSAIISMFELSRKGALSPLIAITVCIGVVLLIAIIIFFEKAQRKLLVQYPKRQVGNKIYGGEATHMPLKLNTSGVIPPIFASSILLFPTTLASFSNSNSDTMSMLTYYLGHGKPVYILLYVVLIMFFSFFYTAIVFNSEETANNLRKYGAYIPGKRPGKNTSDYFDYILTRLTVIGGIYLSVICVIPELLMNKYVISLSLGGTSFLIVVNVVLDTMTQIQTYLFSSKYEGLMKKIKLKN
|
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. {ECO:0000255|HAMAP-Rule:MF_01465}.
|
Q9ZCS7
|
RS13_RICPR
|
Small ribosomal subunit protein uS13 (30S ribosomal protein S13)
|
MARIASVNIPDNKRLVVSLTYIYGLGSTMAAEICNKAKISKDKKVKVLTDQELISLRNIIENEYKVEGDLKREVTLNIKKKKDIRCYQGLRHIRKLPVRGQNTHSNARTRKGKAIAIAGKKKTVK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. {ECO:0000255|HAMAP-Rule:MF_01315}.
|
Q9ZCS8
|
RS11_RICPR
|
Small ribosomal subunit protein uS11 (30S ribosomal protein S11)
|
MNQTIKVKKKKKTITLGVVHIRASFNNTIVTFTDIQGNTISSASAGGNGFKGARKATPYAAQVTIDKASEKAKECGLKTISIRIGGPGAQRESAMRALFGQNFVVTSILDVSSIAHNGVRPPKRRRV
|
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01310}.
|
Q9ZCT1
|
RS20_RICPR
|
Small ribosomal subunit protein bS20 (30S ribosomal protein S20)
|
MANHSSAKKVVRQTVKRTLINKKRSSAIKTFIKKVIHEISRGNKEDANLALSIAQSKIMQGVKKNIIKLNTASRKIRRLSKQIKNLYKSE
|
Binds directly to 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_00500}.
|
Q9ZCT4
|
GRPE_RICPR
|
Protein GrpE (HSP-70 cofactor)
|
MKDYNIENNNVEEENPNVETQVVDNEEIVRLKAEIEELKDKLIRTTAEIDNTRKRLEKARDEAKDYAIATFAKELLNVSDNLARALAHKPANSDVEVTNIISGVQMTKDELDKIFHKHHIEEIKPAIGSMFDYNLHNAISHIEHPDHEPNSIITLMQSGYKIRDRLLRPAAVQVVKKP
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. {ECO:0000255|HAMAP-Rule:MF_01151}.
|
Q9ZCT6
|
CH10_RICPR
|
Co-chaperonin GroES (10 kDa chaperonin) (Chaperonin-10) (Cpn10)
|
MSFKPLHDRIAIKPIENEEKTKGGIIIPDTAKEKPMQGEIVAVGNGVLNKNGEIHPLELKVGDKVLYGKWAGTEIEIKGEKLIVMKESDVFGIIN
|
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-Rule:MF_00580}.
|
Q9ZCU7
|
NTRYL_RICPR
|
Putative sensor histidine kinase NtrY-like (EC 2.7.13.3)
|
MLSDLKQNLRSYFSSRILILALAIASIISVCTTFYVISLEAKNFSTIIGFLLIDLAIFLILGILLTQKFFTKNNDNDSSKLQNRIVIAFSLVAAIPTIIVSVFSVYFFNLSVKAWFDKKISTVLDQSVIVAETYIAEHKVQLKETALAVAEDLSDMYYDLIHNPALFTKTLNTEADMRSLDEAIVLNKSTNTIVANSYLSFSLSFATIPAHLIKKADLGEPVEVKSDPTTIRMLIKLKEYNDVYLLVGRLVDNKIIDHIDATNGAAAEYNSLKNEIDNIQIKFSIMFIFIALLLLFVAINFGVLFTAKIVKPIKKLVTATDKVKDGDLTVQVPENEVDKDEIGTLYAAFNRMIKQLSRQQRDLVIAQRAMAWSDVAKKVAHEIKNPLTPILLASERLLKKFSSEINEKSEFESYLKMIIRHTNDIKNIVSEFVLFARLPAPKFTKSELVYLVKHIIEARKLLNDNIVYTYDSNVDQFDFMCDATQINQVMINVLKNAEESIEGQEFGKIDVILDAKDDFISVIVMDNGKGFPPELIGKATESYVTTSSKGMGVGLAIVKRIVEEHCGVLDIANREDEGAIIDIKFDLKELHLKVRRSGG
|
Member of the two-component regulatory system RP614/RP562.
|
Q9ZCU8
|
RNPA_RICPR
|
Ribonuclease P protein component (RNase P protein) (RNaseP protein) (EC 3.1.26.5) (Protein C5)
|
MKLCITSLKNQKEFELINKLGEKFYERYFILVIAKKLPKIFLESKYNTFLGIKVSRKLNKKAVVRNKIKRRIRHLMRIIVNDSNFKAIKFAIIIIPKKGFEEINFSHLQYELSKIILRNIY
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. {ECO:0000255|HAMAP-Rule:MF_00227}.
|
Q9ZCV0
|
RL20_RICPR
|
Large ribosomal subunit protein bL20 (50S ribosomal protein L20)
|
MTRAKSGKISKKRHKKILKLAKGYRGRANNCFRVAIEKVEKGLQYAYRDRRNRKRDFRGLWIQRINAAVREHGLIYSQFMGALKKAGINIDRKVLAELAVNNNDGFASIVQQSKAHI
|
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity).
|
Q9ZCV3
|
RL25_RICPR
|
Large ribosomal subunit protein bL25 (50S ribosomal protein L25) (General stress protein CTC)
|
MSGILELEAKSRTEFGTGAARALRREGRVPAIIYGAGKTPISISLKEKEITKYYRKPAFISQLINLTIDKKQYKVLPKAVELHPVTDIVRHVDFVFLEAKTQKMEVPIVYEGKERALGVKRGGYFNIIKRRVILLCDVNNIPRNVTIDVTNMPIGTSLKSSQVELPKGCSFITKKEFVLATIIGRRGVKTEIEGEQEVAEAIQ
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01334}.
|
Q9ZCV4
|
PTH_RICPR
|
Peptidyl-tRNA hydrolase (PTH) (EC 3.1.1.29)
|
MILVIGLGNPGTEYQYTRHNIGFIAIERIASKYHLSFSIKKKFNCEIAEAVIDRQKIIFIKPTTYMNLSGKSVILVKTYYNIKYEKVFVIHDDIDLEIGRIKFKTGGGNGGHNGLKSIDVVIGNHYNRIRIGIGRPKNNHDVADYVLNNFSESEYKIAMQSIDNIANNFGLILEHKLAEFTNKIV
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. {ECO:0000255|HAMAP-Rule:MF_00083}.
|
Q9ZCW4
|
MURJ_RICPR
|
Probable lipid II flippase MurJ
|
MTLFRSGIILAFLTFIARIFGLVREQFIASLFGSTPMGDSMNIAFKLPNLFRRIFAEGALSSVFIPIYNEKMLISKKAANNFSGKVFTLLSLTLIVIIALMQIFMPQLILCIAPGFYAKKEKFELTVFLCRITIPYLIFVSLTALLGGILNSVKKFAAFAFSPIILSVCVIIFTLIFGNYIESTISISVSLIIAGILQVVFMFICVKKADLHFPIIFHTNDPDVKKLLINMGPATISSGVQQLNLFISQSISSFIEGAISILAYADRIYQFPLSIIGTSFSTILLPEMSKVYKSNDIVSAQKIQNNAIRIGLLLSLPATFGIIILSHPITNIIYERGVFTPQDTTNTAEAISAFALGLPAFILAKILTPIFYANGDTKTPLKITLFSIIINTNMNLLLMDSLKHIGIAVGTSIAAWYNLGLLYSYSTKQHKLHIEAGIKLFCAKILLCCTLMSIIIALIKHYYLEYLYSEYLLIKVSMLGSTIIIGVAIFFGTAYLLKVVNYDNSTK
|
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_02078}.
|
Q9ZCW8
|
SECD_RICPR
|
Protein translocase subunit SecD
|
MQNLPKWKIVLSIICTVFAIICALPNFIQINSKFLPHDSINLGLDLRGGANLLLDVDFDTYLNDSMENLADTLRKNLRKHKIGYKNLLVRHNNIQLEVRSPEVLKSLKKIINKIDPEIIIGVNKNKIKLRYSESRFNDLLNKVVEQSIEIVRMRVDSTGTKEPTLQRQGNKHILLQVPGSENPSYLKNILGKTAKLTFHLVDENANIEDAIKGHVPLGSMLIKGDSKHHGEYYIVIKKKVLLSGAHLTKASASFDQNSQPIVAFSFNNLGSKIFGEITKNNTGKRLAIVLDNKLLSAPIINGAIIGGNGIITGNFTIESANELALLLRVGSLPTPLKIIEERSIGPNLGADSIESGKKAGLIGFVAVCIFMILSYGVIGLFANIALILALLYILALLSLFQATLTLPGIAGIILTIGMAVDANVLIYERIKEELHKGVSNLYAIRTGFESAFATIIDSNITTLIVAFALYIFGVGAIKGFAVALTIGIISSMFSAIIITKLLIDVWVKYFKPKKLGLL
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. {ECO:0000255|HAMAP-Rule:MF_01463}.
|
Q9ZCW9
|
YAJC_RICPR
|
Sec translocon accessory complex subunit YajC
|
MSQHTQDNQINNNETIEIQETDTVPVETNSLQSGLTSLIPMILIFAVFYFLLLRPQEKRRKEREKLVSGVKKGEEVLINSGIYGIVTKVSENDNNIEIEIAKDVRIKAIKSAIVDITSRKREVAATQENNKKNKKVSCAKSS
|
The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
|
Q9ZCX4
|
RPOZ_RICPR
|
DNA-directed RNA polymerase subunit omega (RNAP omega subunit) (EC 2.7.7.6) (RNA polymerase omega subunit) (Transcriptase subunit omega)
|
MARITAEDCNKIIPDRFRLVVLATRYAKLLNYKVETNQIKKEKRDKPPVISLRRIAAGKVSVPQLEQDLINSLRTRMMIEPLINQDESEDVEEKFEYLPEVYIGEDYSDLDDQIFINENGEDYETDK
|
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity).
|
Q9ZCX5
|
ACPS_RICPR
|
Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS)
|
MLIGVGTDIVQIPRIEKILNIYQELFAKKILALKELKQFTLLNKTNHATFLAKRFSAKEAVSKAFGVGIGRGINFKDITILNDNLGKPTVEISSHYTNKLAPFNIHLSLSDDYPICIAFAIIESNC
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP-Rule:MF_00101}.
|
Q9ZCX9
|
UVRC_RICPR
|
UvrABC system protein C (Protein UvrC) (Excinuclease ABC subunit C)
|
MSLEISGSKLIKAQIIDAPECSGVYKMLDVNKQVIYIGKAKILKKRLTNYIKSDLDNKTLRMISNTYFLEYIITNSEVEALLLEAQLIKKFQPKFNILLKDDKSFPFIKLSLDHDFPQLIKYRGKALSDGKFFGPFASNTQVNTTLTELQKIFKLRSCTDNYFNSRTRPCLQYEIKRCYAPCVGKINKEDYRELVMQVKDFLQCRTIALQANLSKKMQELSSQMRFEEAAEIRDRIKALSYVQLKSGILDVVRDADIIAIVHKNLHYCIEVSLYRAGQPYGAIPYFFSSTENSTHEEVLEYFLLQFYQKQQVPSEIIMNHEINSKENMIEAIKKINNISDLSITVPHKGGKAKLVQKAEVNALLSLEQYLKKSIKNTDIMFALKKLFDLPEIPERIEIYDNSHLQGMFAVGVMVVAGQIGFDKKEYRVFSLSSRSLTIGSEIELRDDRKGDDYGMLRQVLTRRFTRLKNEPHKLPSLMIIDGGKGHLTIVKEVMDKFEINIPFVCMSKGRDRNAGLEQLHMQGKEVLTLDKNLPIMKYLQILRDEAHNFAIKNHRLGRSRAIKISSLDEIDGIGETRKTALLHYFGSYKAVCNATIDELTKVKGISKSLASMIFNILNRKISLDNS
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. {ECO:0000255|HAMAP-Rule:MF_00203}.
|
Q9ZCY2
|
RSMH_RICPR
|
Ribosomal RNA small subunit methyltransferase H (EC 2.1.1.199) (16S rRNA m(4)C1402 methyltransferase) (rRNA (cytosine-N(4)-)-methyltransferase RsmH)
|
MSQYHIPVMLSEVLAVLAPKGYESYLDCTFGAGGYSNAILNSCYCSVTSLDRDPNVIESVEKIKQDYGERFNFIKTNFADSFRKLKHKKFDGIVMDLGVSSMQLDIADRGFSFLYDGPLDMRMSVQGFSAEEFVNTADEEEIADVIYKYGNESLSRRIAKSIVEYRKTARIDSTRKLAEIVRYSIGFRKGKIDSATKTFQAIRIYINNELEELEQFLANVKNILKKDGRLVVVSFHSLEDRIVKNFFKENSEKQVARSKYAKDEIKIDPNKWLKIITPKVLTPSSQEIRLNVRARSAKLRAAKKII
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01007}.
|
Q9ZCY9
|
NTRXL_RICPR
|
Putative response regulator NtrX-like
|
MSQLDVLIVDDEESIRNLIAANLKDEGFNPKIAANSTQALKIISEKPVSAVILDIWLQGSEIDGLGVLEIIKKRYPLMPVIIISGHGTIETAVNAIKMGAYDYIEKPFNNDKLIILLKRACEVTKLKRENIDLKSKVIDKTELVGGCPVTLKYKMEIEKAASSSSRIMIHGKVGSGKELAARLIHKQSKRVNNPFIIFSPTCMTTEKINQELFGESEKQENNNKRPTILEFANNGTLYIDEISNIPIPIQVKLLKFLKDQTITKPCGKKTKVDIKIITSTAKNIQDEVNNGKFLEDLYYRLNVFSLKVPSLYERKEDIPLLVKYFVKQLSKFSGLKERHFSDEAIAALQSYEWPGNIRQLRNVVEWTLIMNPLTTGNNEIIKPYMIPSEILANSANLTKLEDSFDMLSMPLREAREVFERQYLSAQMSRFNNNISKTSSFVGMERSALHRKLKLLSLHIPPTNRINEEEYEKANA
|
Member of the two-component regulatory system RP562/RP614.
|
Q9ZCZ6
|
RIMP_RICPR
|
Ribosome maturation factor RimP
|
MQTIAQQITNIIEESLTDMGFELVLVKFKGVSPKVVEVLIDSLNGNKISIEDCTNVSRTISAILDVEDLIEEAYSLEVSSSGIERTLVKFENYNRFLGREVKIKLKELLNGKTLYPR
|
Required for maturation of 30S ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_01077}.
|
Q9ZCZ7
|
NUSA_RICPR
|
Transcription termination/antitermination protein NusA
|
MSNIYNIEILQIIDSVAREKGISKEILISTVEQAVQVAGRKKYGNEYNIKAQINRKTGEINLLRILKIVEDVEDYLTQISLEDALVKNPEAKIGDEIYEYLPPIDHARVSAQAAKQVITQRVIEAEREKQYHDFKDRKGDIINGIVKRIEYGDIIVDLSRAEAIIKKDQLIKGEHFKPNDRIKAYVQDVRQETKGPQIFLSRVDNQMLVKLFKLEVPEILEDIIQIKSVARDPGSKAKIAVFASDSSIDPVGSCVGIRGNRVKAVTNELNGEKIDIVLWSNDLAQFIVNSLIPLAPSEITKILIDEDSHKVEVVVSQEHQSIAIGRRGQNVRLASKLTGWNIDIMTEEQESKRRNEEFSTSTELFMEALDVEEVIGQLLSVTGFNSVEQIASSEISTLTRIEGFEEELAVEIKNRAIHYVDLKNEKIIKKLEELGVEQELIDILELPLELILKFAEYGIKTIEDLGEMSVNEFKNLAPNSNITDENIKLLIKTARHHGELKDS
|
Participates in both transcription termination and antitermination. {ECO:0000255|HAMAP-Rule:MF_00945}.
|
Q9ZCZ8
|
IF2_RICPR
|
Translation initiation factor IF-2
|
MTDNQEIKPKKLTLGNSKLLLNKSFDSLTGAQSFVNAKSKTLVEVRKSSIGSTTTISLNKERNSLDQSVIDSNKEEFNRRLSILKKAAEQSKLHDPAQISTLSKLASINQSINSKNEQSITDKAVEQKHQNIEDNKVEIAAKIVQDNENISSQIPKKKKETLAKSVLVGMRTRYGIEEEPALEKTVDNKVVVPKIKLEESKKFKKADLFNMLSDDENGSGRTRSLASIKRAREKEKRKLVSQVPEKVYREVTIPEVIGVGDLANAMSERVADVIKELMKLGILANASQTIDADTAELVATNLGHTVTRVQESDVENILINDDKVEDLRTRAPVVTVMGHVDHGKTSLLDALKSTDIAAGELGGITQHIGAYRVTLADSKAITFIDTPGHEAFSEMRSRGAKVTDIVIIVVAADDGIKTQTVEAINHAKAAGVPIIVAINKIDKPDIDIERIKNELYVHEIIGEEAGGDVIFIPISALKKINLDKLEEAILLISEMQDLKASPFGLASGVVIESKIEKGRGTLTTILVQRGTLRNGDIIIAGTSYGKVKKMINDKGREILEATPSVPVEIQGLNEVPFAGDQFNVVQNEKQAKDIAEYRIRLAKEKKISVASRSSLEELLLKASGNSKIKELPLIIKCDVQGSIEAISGSLLKLPSDEIKLRILHSGVGPITESDVSLAHVSSAIVVGFNVRAWANALTAAEKTKVDIRYYSIIYNLIDDVKAIMSGMLEPIVREQYIGSVEIRQIFNITKIGKIAGSYVTKGIIKKGAGVRLLRDNVVIHAGKLKTLKRFKDEVKEVREGYECGIAFENYEDIREGDTVEVFELVQEQRQL
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity).
|
Q9ZD09
|
UBIX_RICPR
|
Flavin prenyltransferase UbiX (EC 2.5.1.129)
|
MIKNKKIIIAISGASGAIYGIRLLKVLKEQNIETHLVISDGAALTIKFETKYSIQEVKFLANYCYDEKNLGAAISSGSFKTAGMIIAPCSMKTLASIAHSMEDSLISRAAGVVLKERRKLILMTRETPLHIGHLENMLKVAHYGGIIAPPIPAFYNKPTRINDIIDHSITRVLDFFDIETNLIKRWSSD
|
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
|
Q9ZD15
|
SODF_RICPR
|
Superoxide dismutase [Mn/Fe] (EC 1.15.1.1)
|
MTYCSKANQPSYPFILPDLPYDKESFKPHFTRETFDYHHGKHHNSYVQNLNNLIKDREELQKKDLEEIIEWSSQNAEVAILNNASQIWNHTFFWYSIKPHGGGKPSGKVFEQISKDFGSFEQFCAQFKQEAVGQFGSGWTWVVYHDNKLQIIKTSNAGTPIVNFMKPILACDVWEHAYYIDYRNKRSDYIDIFIRHMINWKFVEDNLIQ
|
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal ion at the active site.
|
Q9ZD19
|
IF3_RICPR
|
Translation initiation factor IF-3
|
MYLFINIIWRNFISKNNLPKANREIKAKEVRLVDENSEMYGVVNIREALDMAERAGLDLVEISPNAVPPVCKILDFGKFKYESKKRLHEARKKQKVVVLKEMKFKPNISIGDFETKLRKIKEFLKDGDKVKISLWFKGREILHKEVGHELFKRIELALEGLIKIDQHAKMEGKQMIMIVSPDIKV
|
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. {ECO:0000255|HAMAP-Rule:MF_00080}.
|
Q9ZD21
|
RF1_RICPR
|
Peptide chain release factor 1 (RF-1)
|
MSFSDNLVKILDKYENLGKKLSSGIIGDEFVKASKEYAELEDVVVKIKQYNKAKSELEEANNFRLEMALDNATLEMIDNEIHTLENLLPKLERAVRISLLPKDEADSKSAIIEVRAGSGGEEAALFAAVLFNMYQRYSEFKGWRFEILAISDTGIGGYKEASASIKGKDVFSKLKFESGVHRVQRIPETESQGRIHTSAATVAVLPEAEGIDIKIEDKDLRIDTYRASGAGGQHVNTTDSAVRITHIPTGITVALQDEKSQHKNKAKALKILRARLYEEKRRQKEQERSDSRRGQVGSGDRSERIRTYNFPQGRVSDHRINLTLYKIDEVVKHGQLDEFIEALIANDEAKKLSEL
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
Q9ZD26
|
DBHL_RICPR
|
DNA-binding protein HU-like
|
MVTKNYLIDKVHDKLDYLSKQDVKESVDLILDYLNESLKEQKRIEIRNFGNFSIRKRKFPESNKFYNTVYYRMPKNLFKD
|
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
|
Q9ZD28
|
RS1_RICPR
|
Small ribosomal subunit protein bS1 (30S ribosomal protein S1)
|
MSIKLKQRFVPQLAAINCQFEEDFAQMLKTVDTSHIKEKTVVKGQVIEIKNDMIIVDVGLKNEGRIPKSEFLSLPEVGDVVEVFIEKIEGRNGRTILSREKAVKEELWGQLEIMCSKGEFVDGTIFGRVKGGFTVDLSGVVAFLPGSQVDVRPIKDPTSIMNIKQPFKILSMDKKLGNIVVSRRVILEESRSEARDEMLSKIKEGIVLEGVVKNITDYGAFIDLGSVDGLLHLTDISWGRVNHPSEVLEFNQKVKVMVIKFDEKTKRISLGIKQLDSNPWDAIKEEFPVGKKMTGKVTNFADYGVFLELKDGLEGLVHSSEISWLKSNQNPRKMLTIGQEVEFIVLEVDTEKHRVSLSIKQCQENPLIKFAENNPIGTIIKAPIRNITDFGIFVVLGNNMDGMIHEGDISWEDNGTDLLKSYKKGDEIECKVLAINFEKEQVSLGIKQLLPNPYQKISDEYKKSTIVKAVVTEIKDDGLVVLLNNKVTGFIKRVELSDEKDEQKPEMFKVHEEIDAKVVSIEKSTGRVLLSIKAHKIAERQKTLKEYGSSDNTTNMGDILANVLEEKK
|
Binds mRNA thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence (By similarity).
|
Q9ZD29
|
CLPP_RICPR
|
ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Endopeptidase Clp)
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MSYVPVVIEQTSRGERAYDIYSRLLKERIIFVCSTVEDHMANLIVAQLLFLEAENPKKDIYMYINSPGGVVTAGLAIYDTMQFIKPKVATLCIGQACSMGSLLLCGGEHGMRYSLPHSRIMIHQPSGGYKGQATDIEIHARETLKIKRLLNELYSKHTKQELKYIEKSMERDNFMSSEEAKKFGLVDNIISSRDTIAFLAQ
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Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. {ECO:0000255|HAMAP-Rule:MF_00444}.
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Q9ZD44
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RS15_RICPR
|
Small ribosomal subunit protein uS15 (30S ribosomal protein S15)
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MSITTERKQQLIKEYAITENDTGSTAVQCAILTERINNLTEHFKSNHKDHTSRRGLLILVGRRRRLLNYIKKNNVSEYLDLISKLGIRKIK
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One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01343}. Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. {ECO:0000255|HAMAP-Rule:MF_01343}.
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Q9ZD47
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TLCD_RICPR
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ADP,ATP carrier protein 4 (ADP/ATP translocase 4)
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MTINASNIENSFSKINSHFSKLTDYIWPIKRHEISKFLFITLLMFCILFIQNLIRALKDSIVTTMIGAETISFLKFWGVMPSAFLITVIYVKLVNRMKAENIFYLIISIFLTFFALFAYVIFPNHEMLHLRPVTVHNLTASLPNLKWFILLLSKWSFSLFYIIAELWPNVVFALLFWQFVNNITTVEESKRFYPLFGLLSQTGIYLAGHFLENLSNINYYVTNKFALQSSFHTLSIQIILTIVLILGIVSIKTFWLLNHKVLDKKHMALLRFKTKNKSITIAKSFQMILSSRHIRLIATLLICYGIAINLVEGPWKAAATKIYKTPTEYAAFIGSYLSYTGVFTIFFVLLGSNIVRRMGWFTSAVITPSIVFITGILFFAVNNFEGFAGLIIANFILTDPALVAITIGAIQNVLSKSSKYTLFDSTKEMAYVPLEPEIKISGKAAADVIGTKLGKSGSAFLQSLIFIILPSASYQSISICLMIIFILTCVTWIWATKELNKEYKNSIKFSQK
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Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism (By similarity).
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Q9ZD61
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ISCU_RICPR
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Iron-sulfur cluster assembly scaffold protein IscU (Sulfur acceptor protein IscU)
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MAYSKKVIDHYENPRNVGSLDKKKKNVGTGLVGAPACGDVMKLQIEVGDDEIITDAKFKTFGCGSAIASSSLVTEWIKGKSVEDAKEIKNTEIAKELSLPPVKLHCSLLAEDAIKAAIADYKQKRENKKDS
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A scaffold on which IscS assembles Fe-S clusters. Subsequently gives the nascent cluster to other proteins. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters (By similarity).
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Q9ZD67
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TLCC_RICPR
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ADP,ATP carrier protein 3 (ADP/ATP translocase 3)
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MLPPKIFFEKVKEIIWPIERKELKLFIPMALMMLCILFNFGALRSIKDSLVVPSMGAEIISFLKLWLVLPSCVIFTILYVKLSNKLNFEYIFYSIVGTFLLFFLLFAYIIYPNQDIYHPNDAMINNLIASYPNLKWFIKIGSKWSYALMYIFSELWSAVVINLMFWQFANHIFDTAKAKRFYPVLGMVGNIGLIIAGSVLVFFSSGQYIIDSELLTDSYNSSSNNSIMLQPIISIIVTAGIIAMFLFRIINKFILTNSINVLDVKKVAAKTKTKLALIESIKLIIHSKYIGRIALLIICYGLLINIVEGPWKAKIKELHPNTVDYVNFMGMFNIWMGISCVTFMIIGSNILRRLGWLISALLTPIMLSITGFMFFIFIIFIEEIGTCFGDFNLLYVAIIVGAIQNILSKSSKYSLFDSTKEMAYIPLSLELRTKGKAAVEVIGTKFGKSLGAFIQSLIFIIIPTATFDSIIIYLLVIFIVMMNLWIWNIIKLNKEYIKLCQ
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Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism.
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Q9ZDA4
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RECR_RICPR
|
Recombination protein RecR
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MNKTNDIDQLIYLFSKLPGLGIRSARRIVLYLLQDKDVRLKSLINHLIELDKKIVKCEICGNLDTKSICHICSSEYRDKSTIAIVETVAELCAMERSGNFKGLYHVLGHNLSAASRQNPRILRLPELLKRCFVENIKEVIIATNSTLEGQTTAYFIIEYLKEHPAKISRLASGIPIGGELDYLDEGTLSAAISLRQPCE
|
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. {ECO:0000255|HAMAP-Rule:MF_00017}.
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Q9ZDA7
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ISPT_RICPR
|
Isoprenyl transferase (EC 2.5.1.-)
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MTTIKHLAIIMDGNARWADRHNLTKSEGHKAGADKIRELLPEFINLNIPYITLYTFSFENWQRSSSEVDFLIKLLSIYLKNELDSLHENGVKIKVIGRLNLLRSSLQKQINNAIELTKNNNKIKLCIAFSYGSRQEIVDACTKIIAHGKKQVSEYDIQHALYDPEMPDVDLLIRSGGVYRISNFLLWQAAYAELYFSQKYWPDFNKDDIHEAINDYSKRKRTFGKR
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Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. {ECO:0000255|HAMAP-Rule:MF_01139}.
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Q9ZDB3
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DPO3B_RICPR
|
Beta sliding clamp (Beta clamp) (Sliding clamp) (Beta-clamp processivity factor) (DNA polymerase III beta sliding clamp subunit) (DNA polymerase III subunit beta)
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MLKLIVETKTLMQSLGFARSIIEKRNVIPEYANIKLSAQDGNLELSSTNMDLYLSQKIAVQVLNEGEITVATQTLSDIVRKFPDSELTLTEIEITQLEIKGQNCKFNLFTLPVSSFPAMDSIKPEVSFKISCADFAKIIESTKFSISLDETRYNLNGIYLHIKDKEFFAASTDGYRLSISWITLEEKIKNFGVILPQKSAEEILKIVKDPKNIHEDIEILLSSNKIKFICNENTILLSKLIDGTFPDYSAFIPKSSVSKLVINRKIFADSIERIAIITVEKFRAVKLSLSRKILEISAVGEARGTAKEIITASQDKESFYEYNHDESLVIGFNPQYLEDVLKAIKSDIVELYFSDISASAPVLIKFPRNPKDIFVIMPVKV
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Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
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Q9ZDD9
|
YCIB_RICPR
|
Inner membrane-spanning protein YciB
|
MLKLLSEIGPVIAFFAGFFYGGGIQNATLYMLITSIICITLCYIIDKKVSKLSIISSTVLFISGIITLISGDSMYIKIKPTILYVIFGIIFLMSGIKKNPFIKYALESIVRLKEESWIILSYRTAAFFFFMAVVNEVVWRNFSDETWVKFKVFGVIPITFIFILLQLPLLLKNKLPDSKI
|
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. {ECO:0000255|HAMAP-Rule:MF_00189}.
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Q9ZDE1
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RLPA_RICPR
|
Endolytic peptidoglycan transglycosylase RlpA (EC 4.2.2.-)
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MIIMRNYKFKLEPLKQCQEAFKRYTVHSTALYIIALQANWSRRLIYKLSLYFCKIKNCYTTFKFEQSNRFIITKAERIIKIQHLIRFKDIVNNFISLINILLVLIFCINLSGCNASKKLSYSNKYSYKELSKDDPHNLTYIGHYKVGKNYKIKGKIYKPHTPKYFTETGYASWYGGRKDGFHGKTTANGDRFNRNLLTAAHKTLPLPCLVKVTNKVNNKSVILMVNDRGPFKKNRIIDVSQKAAEILAFKNQGVTKVRIEYLPNETEKFLKKINLKKPENKTFAKNHKKSLFTQITKNNQCSINCHIKLVNLKYKLAVNP
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Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. {ECO:0000255|HAMAP-Rule:MF_02071}.
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Q9ZDE6
|
RUVA_RICPR
|
Holliday junction branch migration complex subunit RuvA
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MIGKLNGKIDSHCDDYVIIDVNGVGYLVYASGKTLAKLVEGKFYKLFIETHVREEHIHLYGFLTLEEKNFFNLLQSVNGIGTKMALSILSNLTPTDIQIAINNDDRNIFKAISGVGAKLAERIMLELKDKITKIFSSSAIIKDSNISSIAINEVMKALVNLGFTRFEAQNTVQGIITQNPKISIDELIKTALKNRNSSF
|
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA. {ECO:0000255|HAMAP-Rule:MF_00031}.
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Q9ZDE7
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SYP_RICPR
|
Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)
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MLLSKYFLPILKEEPSEAKVISHKLMLRSGMIMKQAAGLYTWLPLGLKVLKNIENVVRSNMNKVGALEVLMPCIQPAHLWIESGRFEHYGKEMLKFQDRHDNTLLFGPTNEDMITDIFRRNIKSYKDLPKNLYHIQWKFRDEIRPRFGVMRGREFLMKDAYSFDINQKNAVNTYNKMYKAYMNTFRDLGVFAIPVIADNGPIGGNLSHEFHIVAETGESTIYYDKRFKILKDNPDIDVEEIKGWYAAAEEKHDVNKLSSFPEGITRSKGIEVGHIFYIGSKYSVNMNALINDEYGKLIPVEMSSYGIGISRLAAAIIEANCDKKGIIWPCSVAPFKVSLINLNIHDNKCVELAAKTDKELSHQNIEVLYDDTDARPGSKFATHDLIGSPYQIIIGPKKAANNIVELKDRKTGVLEDIEVENIINYIKNIDSI
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Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). {ECO:0000255|HAMAP-Rule:MF_01570}.
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Q9ZDF0
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KDSB_RICPR
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3-deoxy-manno-octulosonate cytidylyltransferase (EC 2.7.7.38) (CMP-2-keto-3-deoxyoctulosonic acid synthase) (CKS) (CMP-KDO synthase)
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MKNQDVAIIIPSRLNSTRLIQKPLQLIGSITLIERVFQQVNKANIHHTYVATDSEEIANVIKKISGKVIFTDSNIPTGTDRAYEAFKLIPNNHNIHYIINVQGDIPFIEHRSILKIIEYLKNSEYDIVTPVVKVDRESIEDSSNVTVAVDYTGKALYFSRSPIPHGAEEFLYHLGIYGFRKNALEKFVSLKQTFLEKTERLEQLRILENGMTIGTCLVENVPISVDTEEDLKKAIKFCKKINKLGL
|
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.
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Q9ZDF2
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TLCB_RICPR
|
ADP,ATP carrier protein 2 (ADP/ATP translocase 2)
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MNIVDSNCTIWHKARNSKFRHIVWPIRSYELTKFIPMTLLMFFILLNQNLVRSIKDSFVVTLISSEVLSFIKLWGEMPMGVLFVILYSKLCNIMTTEQVFRIITSTFLFFFAIFGFILFPYKEFFHPNPELINQYIIVLPHLKWFLIIWGQWSLVLFYIMGELWPVIVFTLLYWQLANKITKVEEAPRFYSFFTLFGQTNLLFSGTVIIYFAKSEHFLLPLFAHLNDTNEILLKSFITVILISGLICLALHKLIDKSVVEADKNIKFKNQRTDILKLSLLESAKIILTSRYLGFICLLVMSYSMSINLIEGLWMSKVKQLYPATKDFISYHGEVLFWTGVLTLVSAFLGSSLIRIYGWFWGAIITPIMMFVAGVMFFSFTIFEQHLGNIVNTLGYSSPLVIIVFIGGLWHVFAKSVKYSLFDATKEMVYIPLDNEIKTKGKAAVDVMGAKIGKSIGAIIQFISFSIFPNAVHNDIAGLLMVTFIIVCILWLYGVKVLSQNYNKMIKR
|
Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism.
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Q9ZDF3
|
MDH_RICPR
|
Malate dehydrogenase (EC 1.1.1.37)
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MKKNPKISLIGSGNIGGTLAHLISLKKLGDIVLFDVSEGLPQGKALDLMQAATIEGSDIKIKGTNDYRDIEGSDAVIITAGLPRKPGMSRDDLISVNTKIMKDVAQNIKKYAQNAFVIVITNPLDIMVYVMLKESGLPHNKVIGMAGVLDSSRFNLFLAKEFKVSVKNVNSIVLGGHGDTMVPLLRYSTISGVPIPDLIKMGLSSNKNIEKIIDRTKNGGGEIVKLLKTGSAYYAPAASAIAMLESYLKDKRQILTCAAYLQGEYDIHDLYIGVPIIIGKEGVIKVIELQLTEEEKILFYKSVTEVKKLIDTIQ
|
Catalyzes the reversible oxidation of malate to oxaloacetate. {ECO:0000255|HAMAP-Rule:MF_00487}.
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Q9ZDH3
|
NUOC_RICPR
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NADH-quinone oxidoreductase subunit C (EC 7.1.1.-) (NADH dehydrogenase I subunit C) (NDH-1 subunit C)
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MTLDKLIEKLAAKFRIVITKVAVKDHLAYKIEPHFLLPFLKALKESEELRFTVLTDLFGVDFPKKEKRFEVVYNLLSLKLNKNLIIKTHISEKESIPSAMQILSAAYWYELEVYDMYGVNFNGNNDKRRILTDYDFEGHPLRKDFPLTGYTQVKYDKKLEKVTYEPVNLDIEYREFDFSSHWHSPSYVLPGDEKTEE
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01357}.
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Q9ZDH4
|
NUOD_RICPR
|
NADH-quinone oxidoreductase subunit D (EC 7.1.1.-) (NADH dehydrogenase I subunit D) (NDH-1 subunit D)
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MTNKTITLNLGPQHPATHGVLRLILEMDGEVVNNADPHIGLLHRGTEKLIEHKTYLQAIPYFDRLDYVSPMCQEHAFALAVESLLECSVPRRAQFIRVLFSELTRILNHTLNIGSQALDIGATTPLLWLFEEREKIMEFYERVSGSRMHSNYFRPGGVAEDLPENLLEDINKFIEQFPSKLNDIENLLNENRLWKQRLVDIGVVSQKDAMDWGFSGPMLRGSGIAWDLRKSNPYDVYDEMDFEVPIGKNGDCYDRYLVRILEMYESIKIIKQCIVKMPKGQVKTDDPKLTPPTRGKMKESMEAMIHHFKLYTEGYDVPIGETYKAVEAPKGEFGVYLYSQGGNKPYRCRIKAPGFAHLQGLNFMSKGHLIADVITIIATLDIVFGEIDR
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NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01358}.
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Q9ZDH5
|
NUOE_RICPR
|
NADH-quinone oxidoreductase subunit E (EC 7.1.1.-) (NADH dehydrogenase I subunit E) (NDH-1 subunit E)
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MNTKITNFTFAFDKKNLNLAETIIKKYPPEGKRSAILPLLDLAQRQNGGWLHVSAIEYVANMLEMPYMRAYEVATFYTMFNLNPIGKYHIQVCTTTPCWLRGSDNIMKICEKKLAIKHKETTKDQKFTLSEIECLGACVNAPVVQINDDYYEDLNEAKMEKLIEQYLNEFKSKMQNG
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
|
Q9ZDH8
|
EX7S_RICPR
|
Exodeoxyribonuclease 7 small subunit (EC 3.1.11.6) (Exodeoxyribonuclease VII small subunit) (Exonuclease VII small subunit)
|
MTNTKTLKDNISFEEALRELEEIVKKIDTGQENLETAVNSFERGILLKNHCEKKLKEARLKIEKITKLADSTVILEETEV
|
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. {ECO:0000255|HAMAP-Rule:MF_00337}.
|
Q9ZDI0
|
RIMM_RICPR
|
Ribosome maturation factor RimM
|
MNSLKNLILIGVIKSCHGIQGHVILKSFTEPSTKILERTLVNESGANIRIKLISQNAKGELICTFNDIATRNEAENLKGYKIFCLRTSLPKLEEDEFYIADLNHLQILDQSNKEIGKIKNILNFGAGDIIEIEFLDKTTELLPFNKEFFPIITKDYVILNYQTKV
|
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00014}.
|
Q9ZDI3
|
RS4_RICPR
|
Small ribosomal subunit protein uS4 (30S ribosomal protein S4)
|
MTKIVRSKYKASRRLGVSLWGDSKDAFNTRNYRPGQHGQNTMIKTSDYGLHLKAKQRLKCYYGRVTEKQFRNIFALAQRMKGNTGENFIGLLESRLDTVVYRMNIAPTIFAARQLVSHGHIKLNGKKADIASIRLKEGDIIEIKESIQQIPLIQESISKQGQTTPGYLSFDIPSLTGKYLRVPALSDVPYPFEAEVHLVIELYSR
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01306}. With S5 and S12 plays an important role in translational accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}.
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Q9ZDJ5
|
CAPD_RICPR
|
UDP-glucose 4-epimerase (EC 5.1.3.2) (Galactowaldenase) (UDP-galactose 4-epimerase)
|
MFVDKTLMITGGTGSFGNAVLSRFLKSNIINDIKEIRIFSRDEKKQEDMRIALNNSKLKFYIGDVRNYQSIDDAMHGVDYVFHAAALKQVPTCEFYPMEAINTNVLGAENVLSAAINNKVTKVIVLSTDKAVYPINAMGLSKALMEKLAIAKARMRSPGETILCVTRYGNVMASRGSVIPLFIHQIKQGKELTITEPSMTRFLMSLVDSVDLVLYAFEHGRQGDIFVQKSPASTIEVLAKALQEIFGSKNAIRFIGTRHGEKHYESLVSSEDMAKADDLGGYYRIPMDGRDLNYAKYFVTGEKKVALLDDYTSHNTKRLNLKEVKELLLTLDYVQKELKNA
|
Epimerizes UDP-galactose to UDP-glucose. May contribute to formation of LPS or the exopolysaccharide slime layer by providing UDP-galactose as a substrate for either molecule.
|
Q9ZDJ8
|
YQGF_RICPR
|
Putative pre-16S rRNA nuclease (EC 3.1.-.-)
|
MIIKNLQEFYRLLIPNKPLIAIDYGSKKIGVALSDQELSIAMPFNTITAVNKKVVITSLLNIIKKYKVCGIVIGLPIDMSGGVTQQTNIVMKFAEKLKQSLGLPIYLQDERLTTKSANNFLKSFGIKRKDRNHNDDAVAASMILEIVLNAIKRFNL
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00651}.
|
Q9ZDK4
|
BIOY_RICPR
|
Probable biotin transporter BioY
|
MRYIMNSLFKILYLNRFVEYLSTNTYILDIVKIVMGVIAIFASSQITIPIKPVAITMHSVILCIIAFTYSPRLSFLTILTFIFIGVMGLPVFCQFSSGINYFLGSAGGYYLGFLIGMPVMSVLKGKLAENYLNVTIICIIGHAIFYLCGIIWLASMIGLKQAIYSGFIIFIPSGLVKILIFSCLFSYIKNLKRK
|
Probable biotin transporter.
|
Q9ZDK5
|
CYAY_RICPR
|
Iron-sulfur cluster assembly protein CyaY
|
MNNTAFSKLAETTIVYIVDKIEEQDLEGIIDVDLQGDILNLDTENGIYVINTQSASKEIWLSSPVSGPHHFFYEQGKWKSRIGFELMVLLTEELGIRFDKYEIF
|
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. {ECO:0000255|HAMAP-Rule:MF_00142}.
|
Q9ZDK7
|
LPXB_RICPR
|
Lipid-A-disaccharide synthase (EC 2.4.1.182)
|
MKKIYFIAGEMSGDFIGGHVIQNLKSNEGLEFTGIGGKYMEEAGNFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHIINSKADLLITIDSPGFTYRVAKRVRKLLPNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYIGHPIMEQEFYRDKIALRKELKIDENERILCVTLGTRKGEILRHLPIFIDAIQEISKDYKNLTIIFPLAHPDHEAIIKPFLDNIQFNYLFLSNERLKAYAVSDLALAKSGTNTLEISASGTPMVVAYKVNIISFIIIMLLIKIKYVSLINIIAGSEIIPEFIQFNCKANLISNKLKELLSNSQKRYNQVVKSKKILQKLGFESNRSPSYIAAKIIKQEFL
|
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q9ZDM3
|
COXZ_RICPR
|
Cytochrome c oxidase assembly protein CtaG
|
MSKKSNKNLAFSLLGLMMSMVLLSFASVPIYNLFCKVTGYGGTTIKETVSVYSKVKGTKAIIIEFDANVDPNLPWHFIPRQKRVQIVPGQNTLVFYEAENLSNKDIIGTSIYNVTPNKAGKYFVKIHCFCFEEQLLKAREKVLMPVTFYIDNDFERDPEMENIKVITLSYSFFKIREL
|
Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
|
Q9ZDM5
|
TOLB_RICPR
|
Tol-Pal system protein TolB
|
MRNIVYFILTLFSLTSYALETINIEHGRVDPTPIAVNKFNADSSNNDLVGRDVVKVISNDLKISGLFRPISSASFIEEQTGIKYKPLFAAWRQINASLLVNGEVKTLENGKLKISFILWDTFLEKQLTGALFEVPTKLWRRAAHKIADKIYEKITGDPGYFDTKIVYVSESTVLPKIKRIALMDYDGANNKYLTNGKSLVLTPRFAHSADKIFYVSYATKSRALVYEKDLKTGKESVVGDFVGISFAPRFSPDGKKAVMSIAKNGSTHIYEIDLATKQLNKLTNGFGINTSPSYSPDGKKIVFNSDKNGVPQLYIMNSDGSDVQRISFGVGSYASPSWSPRGDYIAFTKIIRQDGEKTFNIGIMKAYPQDHGNSERIITSGYLVDSPCWSPNGRVIMFSKGWPSKANAPGKNKIFTIDLTGHNEREIITPADASDPEWSGILN
|
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. {ECO:0000255|HAMAP-Rule:MF_00671}.
|
Q9ZDM9
|
MUTS_RICPR
|
DNA mismatch repair protein MutS
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MTLCNMNLHEFRQKYNYNVATKMMQQYLDIKFAHLDCLLLFRMGDFYELFYEDAILASNILGIALTKRGKNCEEEIPMCGVPYHALEHYLTKLIEENYKVAICDQLETPEEAKKRDGYKAVVTRDVTRIITPGTIIEENLISVTEPNYLTSLVIPKNKKTASICCVDLSTSKIFVINVPETEILNELARLKSREILLSENLKSSNISDSILKQFNCRITYQVDSFFAINKCEKIILDFYKIRDIKGIGEISNSQICAIGSILEYLSLTQKQNIPHLPIPKIINFHNYMTIDFSTRRNLEIVTNLQGNLYGSVLNTLNHTVTTQGGRLLYHFLSSPLTNIAKINHRLNITEFFYSNLGIVTRIRELLKNTSDIERCLTRITMNRSSGRDLLSIKYTLETAKTIKGLFSESYGLNLPHFIEKIIKPLSGDAELYNLIHMSIREDAPNNLNDGGIIKYEFHPKIAQLNDLINNKKLHVEKLKDQYRKETRIESLKISHNNVLGFFIDITPKNVNKILDPKFIHRQTTINSVRYTTYELQNLENELVNAQTLVIRLEKELYTDICRKVIEKSSYLKILANSLSGLDVFCNFAYIADEYDYTKPEFTNDLSFDIVKGRHPVVEAALRKTSKSFVYNDCHLSEAERIWLITGPNMAGKSTYLRQNAIITIIAQIGSFVPAKSAKIGVVDKIFSRIGAADDLIKGQSTFMAEMLETSAILAQSTKNSLIILDEVGRGTSTYDGVSIAWSVLEYIHDKLQCRCLFATHYHELTVMKNFLPALQNYTIAIEESGKDILFLHNIILGASNKSYGLHVAALAGLPTSVINRAAQILLKFEKISISKEKNILSNASNNLSLFNFEHEKPISNSKLDEEFKTIDPDKISPKEALELIYKFKKLV
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This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity (By similarity).
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Q9ZDQ2
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RF2_RICPR
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Peptide chain release factor 2 (RF-2)
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MRAEIENYIKKIEQSLDLIWRSLDIEALTVRLTELEELTADPNLWNNNANAQTLLREKNNLEEKLNVFNKLKSNLKEILELEAMAEVENDLETLNQIEQDFKKLSIITAKFETECLFSGETDCNNCFLEINAGAGGTESHDWASIMMRMYLRFAERLGFKTKIINMINGEEVGIKSCTIRIIGKRAYGWFKTESGVHRLVRISPFNAAGKRMTSFASSWIYPEIDDDIAITIEDKDLRIDTFRSSGAGGQHVNTTDSAVRITHIPTNTVTQCQSDRSQHKNKAQAMKMLQAKLYKLEMQKRNENVDKQNANKTDNSWGHQIRSYVLQPYQIVKDLRTNYETSDTKGVLDGNLEDFVSASLSMNNSGNKT
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Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
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Q9ZDR3
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ODPB_RICPR
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Pyruvate dehydrogenase E1 component subunit beta (EC 1.2.4.1)
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MQITVREALRDAMQEEMLRDEKVFVIGEEVAEYQGAYKVTQGLLEQFGSKRVIDTPITEYGFAGLAVGAAFAGLRPIVEFMTFNFAMQAFDHIVNSAAKTHYMSGGQVKCPIVFRGPNGAASRVAAQHSQNYTACYSHIPGLKVVAPYSAEDHKGLMLTAIRDDNPVIFLENEILYGHSFDVPDIIEPIPFSKAKILKEGSNVTIVTFSIQVKLALDVVNILQNDNIDCELIDLRTIKPLDTDSIIESVKKTNRLVIVEEGWFFAGVGASIASIVMKEAFDYLDAPIEIVSGKDVPLPYAVNLEKLAMPSANDLIEAVKKVCYYSI
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The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
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Q9ZDR4
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ODPA_RICPR
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Pyruvate dehydrogenase E1 component subunit alpha (EC 1.2.4.1)
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MDIKPEKYKPIKEEYIKSFKDMLLLRRFEEKCGQLYGMGKIGGFCHLYIGQEAVISAVAMIKKKGDSTITSYRDHAHIILAGTEPKYVLAELMGRATGCSKGKGGSMHLFDIPNKFYGGHGIVGAQVPIGTGLAFAEKYNGTNNICFTFLGDGAVNQGQVYEAFNMASLWGLPIVYIIENNEYSMGTSVARSTFMCDLYKKGESFGIRGFQLDGMDFEEMYNGTKQVAEYVRENSFPVILEVKTYRYRGHSMSDPAKYRSKEEVEKYKERDTLVRIREIILDNKYATEADLKAIEQSVREIIKVAVEFSENSPLPAEDELYTEIYV
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The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
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Q9ZDS2
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CYCM_RICPR
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Cytochrome c homolog
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MTGKELNKIVAAILFASLIAMIVGFIANILYKPNLHVLHRGYSIAIQKSSSNESATVIAQESVNIQELMKTANANHGREIAKKCLMCHSLDKDGPNKLGPHLWNIVGRPKASITDYKYSFAISKLGGVWDDENLFAFLHKPSSYAPGTKMSFAGISKPQDIADVILFLKNYVHDQ
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May be involved in electron transfer from bc1 complex to aa3.
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Q9ZDS5
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FTSQ_RICPR
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Cell division protein FtsQ
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MRQKTISNKNKQTKNTNNISLRRKLGLMYKKAILVLKIVLMIFVCLFVFTKYFTSIKTYLITNIYQVTTKLGFRLENVIIEGQQNVDELTILKVLNANKSSPIFSLKLDEISNNLKKSKWIKEVYVSRRLPNTVYIKLFEREPIAIWQINNQLFLIDEEGYKISKDIQPFSHLLHVVGEGANIYASKLVLELQKYPALLNKTLVAIRVGDRRWDLNLKGNISIKLPEKEFETALKYIDALNKTNKLFNQNYKALDLRDRNKYYIQKY
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Essential cell division protein. {ECO:0000255|HAMAP-Rule:MF_00911}.
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Q9ZDT7
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EFP_RICPR
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Elongation factor P (EF-P)
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MKISANSIRTGNILVYNNDLWVVSKTPEHTQPGKGGAYVQVEMKNLKTGTKRNDRFSSSDYLEKAELEQKDCQFLYFEGNNLVLMDTKHFDQINVPKEILEAKLPFLTENMIVKVEFYNDKPLTIVLPPTVILAISETDPVIKGATVTSSYKPAILENGIKVKVPQYLAIGEKIVVKTDDMTYVERAK
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Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).
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Q9ZDU1
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RL13_RICPR
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Large ribosomal subunit protein uL13 (50S ribosomal protein L13)
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MKTYSAKPSEIEKKWWVIDAKNVVLGRLASRVAIMLRGKHKPSFTPHLDCGDNIIIINAEHIKLTGKKLNPKDGKVYYRHTGFPGGIKDTTAGKILSGKYPERVIKMAVKRMITRNVLGAKQMSNLYVYANCEHPHMAQQPTIYDFASENPKNKK
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This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. {ECO:0000255|HAMAP-Rule:MF_01366}.
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Q9ZDV6
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QUEA_RICPR
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S-adenosylmethionine:tRNA ribosyltransferase-isomerase (EC 2.4.99.17) (Queuosine biosynthesis protein QueA)
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MKLSDFDFNLPSALIAQYPSSERDNSDLLIAGTKHIKTKFYNIIDYLKKGDLLVFNNSKVIKAKLHLGKNITINLNKKLSDNCWIAFAKPARKLNIGDEFYFDTHKIIITEKLAIGEIKVKFMLDNISIIKFLDKYGEIPLPFYIKRPSPVCYSNMALCCKPENTLKIKSIPHNMSKIVTNNSNTVNLRSNDGIIDSTNDNDRYQTIYSQIEGSVAAPTAGLHFTKNILDKLKTKGVHTAFVTLHVGAGTFLPVKTENIHEHKMHTEYCSITTETAEIINKTKQEGRSIIAVGTTTLRTIESACNNGIVRAGNFETDIFITPGFNFQVVDMLLTNFHFPKSTLFILICAFAGFKEMHALYKYAIKEKMRFFSYGDATLLYRKV
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Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). {ECO:0000255|HAMAP-Rule:MF_00113}.
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Q9ZDV8
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DEF_RICPR
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Peptide deformylase (PDF) (EC 3.5.1.88) (Polypeptide deformylase)
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MSIFSIVTAPDERLKQKSKPVLECTDQTRKFMHDMLETMYNADGAGLAAVQVGILLRILVIDIKEYDPVERPKDFYPLFIVNPEIIEKSTELVTANEGCISLPKQRIEVTRPESVKIRYLDYHGKSQELKANDWLARVIQHEYDHLEGKLMVDYLSNLKRDVVLRKLKKLKNNIV
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Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).
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Q9ZDW1
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GLRX1_RICPR
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Glutaredoxin 1
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MNKSILHTIIIYTLASCPYCIKAKALLDKKNVIYEEIEVSNLTQEEKEKFIKKSGGKSTVPQIFIDNMHVGGCDDLFNLEKEGRLDKLLEHQPKN
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Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity).
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Q9ZDW4
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HSCB_RICPR
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Co-chaperone protein HscB homolog
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MQNYFQLLELPQEYNIDLKILEKQYFAMQVKYHPDTAKTAQEKAQNLITSTELNKAYSTLKDALKRAEYMLLLQNINLNDEKIRSLLSPLELSIFWDEMERIENTTLFSDLEKLKNKYELMQQQNINSLKQAFVEQNLSDATIYTSKLKYIRTLQSKLQEKIKSCK
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Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA. {ECO:0000255|HAMAP-Rule:MF_00682}.
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Q9ZDW5
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HSCA_RICPR
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Chaperone protein HscA homolog
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MQIIEITEPKQTDFQQKLQIAVGIDFGTTNSLIAIATNRKVKIIKSIGDKELIPTTIDFINEDLIIGNNKGLHSIKRLFGKTLKEILNTTTLFSLVKDYLDINSSELKLNFANKKMRIAEIAAEVFIYLKNQAEKQLKNNITKAVITVPAHFNDAARGEIMLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQTGRYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGDDIDVVITQYLCNKFDLPHSIETLQLAKKAKEILTYKESFNNDIISINKQTLEQLISPLVERTINITQECLEQSGNPNIDGVILVGGTTRIPLIKDELYKAFKIDILSDIDPDKAVVCGAALQAENLITQHTNSLLIDVVPLSLGIELYGGIVEKIITRNTPIPIAVIKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGNIRVEVTFAIDADGILSVSAYEKISNISHNIEIKPNHGINKTEIETMLKNAYKNAKIDYTTRLLQEAVIETEALMSSIERSIIKLTKLLSESEISIINALLDNIKDAVQTRDQILIKNSIKEFKSKIKKYLDTKLNINDLRKCKNSNQIK
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Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (By similarity).
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Q9ZDW6
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FER2_RICPR
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2Fe-2S ferredoxin (Adrenodoxin-like protein)
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MLRKIKVTFIINDEEERTVEAPIGLSILEIAHSNDLDLEGACEGSLACATCHVMLEEEFYNKLKKPTEAEEDMLDLAFGLTDTSRLGCQIILTEELDGIKVRLPSATRNIKL
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Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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Q9ZDX9
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DNAK_RICPR
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Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70)
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MGKVIGIDLGTTNSCVAVMEGKEPKVIDNAEGERTTPSIIAFANSERLVGQPAKRQAVTNPRNTIYAVKRLIGRNFTDPMVRKDQGLVPYNIVKADNGDAWVEADNHKYSPSQISAFILQKMKETAENYLGEKVTQAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGFEKSSSKTIAVYDLGGGTFDVSILEISDGVFEVKSTNGDTFLGGEDFDTRILNHLIEVFKKESGIDLSKDPLALQRLKEAAEKAKKELSSTSTTDINLPYITADSTGPKHLNIKFTRAELEKLVDDLIEKTIEPCRQALKDAGFKPNDIQEVVLVGGMTRMPKVQEAVKKFFGREPHKGVNPDEVVALGAAIQGGVLNKEVTDILLLDVTPLSLGIETLGGVFTRLIDRNTTIPSKKSQVFSTADDNQHAVTIRVFQGEREMAKDNKLLGQFNLEGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKASGKEQKVTIQASGGLSDAEIEQMVKDAEHNADEDKKRKELIETKNAADSLVYSTEKTLREYGDKLSSEEKGTVEEALTSLKAALESEDASLIKEKTGNLTAANMKIGEAMYKTQTENQHSEANTVNNEKVVDADFQDVDKK
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Acts as a chaperone.
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Q9ZDY1
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BAMD_RICPR
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Outer membrane protein assembly factor BamD
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MKLTKLLSALLVIGLVLGGCKSKKDSNDIVAPIATLYNEGIILLDKKKYKKAAEEFGKIFYQHPGNEMTPQAELMQAYSLFLAAQYEEAVDILNMFINLHPANIDIAYAYYLKALSYYMLISDVNHDQSRTFLSKDSFEDVITKFPNTKYAIDSSLKIDLVNDHLAGKEMMIGRFYLKKKNPMAAINRFEEVIDNYQTTYHSVEALYRLVESYMMLGLHDEAKKYTSVLGYNYPNSKWYSYAYRLVKNYQN
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Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. {ECO:0000255|HAMAP-Rule:MF_00922}.
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Q9ZDY2
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RECN_RICPR
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DNA repair protein RecN (Recombination protein N)
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MFYSLSVKNFILIDELEIEFSKGLCVITGETGAGKSILLDAILFCLGYKTSNNIIKHGKDYTVVNIIFSLNEKIKKFLIQNFIEPEELLLVKCLQKAEGRKSFFINNQIVTKTLIKQLANYLFELHGQNNNITLLEASTQRDILDSYGDLLEFRVKLAKCYQIWQNTRKEIEEITVKQNVIEQEIDYLNFVTEELTKLNIQIGEEETLTNIRQDLQNKNKDLQLIRDIIAQINNPEINISINRAEKLLARQRDNDRFKAIATSLEEAYNNLEVARQELSNLLDSFTYEEYNLEETEERLFLIKAISRKYNVPANELGIFLDKSLEKLVILKNKIANSHKLQAQEVLLQEQYYKLANDLSARRLIAAKHLEESLNQELKQLKMEKANFKIEIKTAIDPTASGNDDIVFKASTNPGMKAEEINKIASGGELSRFMLALKTSLFDKMIKPSIIFDEIDVGIGGEAADKVGDRLKKLSSVTQVIVITHQPQVAGKADLHIKIEKTQLEQETKIKVKALNLAERQRELARMISGKTITDASLKVAKELLYPVACPHDQK
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May be involved in recombinational repair of damaged DNA.
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Q9ZDY3
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ODO1_RICPR
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2-oxoglutarate dehydrogenase E1 component (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase)
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MEEYFNKTGYLFSGNAVFVEELYRQYLANPNSVDQTWQEFFADIKDNNVVLNKSTAKVISTNVTNKELLNNNLSSETLNNLKAKEMISAYRRNAHYLANLDPLGLEIRKTKNDLKLNIEAFGLDSSQLGENINIMDEFIGTWNCKLSELVTKLDKVYTSSIGVEFDQIENVEEKNWLYTKLETDITFTSEEKKSILNDLVEVECFEQFLHIKFPGAKRFSIEGGDASIVAMNKAIDLSMHQGVEEIVIGMAHRGRLNTLTKVVGKPYKEVIASFINGNIFPDGLNVSGDVKYHLGYSADRVRANQKIHLSLADNPSHLEAINSIVAGKVRAKQDIFVDTKRSKIKAILVHGDAAFCGQGVVAESLSMSPLTAYNVGGILHFVINNQLGFTANAADTRASRYSTEFAKIISAPILHVNGDDIEAVLKATDIAVEYRQKFSKDVVVEIICYRKYGHNEGDEPMYTQSKMYNIIKSKPTPGSIYANELVKNGIIDNNYYAKLKEKFKIRLDQEYEQAKSYKQETHFFEGYWKGISRIRGKDAITGVNKKILQDLGTKLCEIPKDFAINPKLIRLFEVRKTTLTTDQPIDWATAEQLAFAHLLCSGINIRLTGQDSARGTFSHRHSILHNQIDDTTYIPLNNLSKTQAKYEVANSNLSEYAALGFEYGYSLANPKNLVLWEAQFGDFANGAQIIFDQFISSSATKWLRMSGLVVLLPHAFEGQGPEHSSARLERFLQLAAEENMYITYPTTPASIFHLLRRQILESTRKPLIVMSPKSLLRHKYAVSKLDELGENTTFIPILDEVTKIDTNNVTKVILCSGKVYYDLFAMRTNNSNIVIIRLEQLYPFEKKLVASLLKKYNKAQAFIWCQEEPKNMGAWHYIATHLNDALKEAEINNEFKYVGREESASPAVGSLQVHNKQQEKLLMEALGDDIIKEKLY
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E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
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Q9ZDZ2
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DBH_RICPR
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DNA-binding protein HU
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MNKTEFIAFMTEHGHNNKHAAHKTLTKADAEKALNLVIESVISAIKSKHNVNLTGFGSFEIHHRKEREGRNPKTGAKMKIDAYNQPTFRAGRKLKEACN
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Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
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Q9ZDZ5
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RSME_RICPR
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Ribosomal RNA small subunit methyltransferase E (EC 2.1.1.193) (16S rRNA m3U1498 methyltransferase)
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MKYNRIYINSNLAENSKLELARDYVHYVKTVLRLKIHDSLRIFNGSDGEFLAQITQIGKNNLSVVLKEQLKKAYIESALTLAVAIIKSDKLMLTINMATQLGITKIIPLITRRCQFRTVNIERLMKCVIEATEQSERLNPPIIEQAITLKDYLKKNNNLILYANEHEKVKHSILHISSLLSKDIAIIIGPEEGLLMMS
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Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
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Q9ZDZ7
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RATA_RICPR
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Ribosome association toxin RatA
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MLSFQHTKILPYKPKKLFDLVWDIKSYPQFLPWCAAARIISENNQEVISELVIQLKGLSEKYNSRVINTITDNGIYLIDTVAISGPFEYLKSTWQFIPHSTGTELKFFINFKMTSVILDKLIGSYFTIATEKMILAFEKRAKEVIK
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Toxic component of a type II toxin-antitoxin (TA) system. Binds to 50S ribosomal subunits, preventing them from associating with 30S subunits to form 70S ribosomes. Its antitoxin is unknown (By similarity).
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Q9ZE01
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NUSB_RICPR
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Transcription antitermination protein NusB (Antitermination factor NusB)
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MSTNKINKKSIARIAAVQALYQNILQNNYDMYDIMQNILACYHSNNSIDLPKNFKISLSISHFKMLVKSVFENINKLDEIIDNHLTNAKDSVHMPILLRALLRVSICELLFCSTTPAKVVINEYTDIANDLLNEHEIGFVNSILDKIAQENNKIS
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Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons. {ECO:0000255|HAMAP-Rule:MF_00073}.
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Q9ZE08
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RRF_RICPR
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Ribosome-recycling factor (RRF) (Ribosome-releasing factor)
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MEKDNLKKILQEKMEKAIKVLGNELKGLRTGRASINFLDSVTVEAYGSKIPLSQVASLSTPDARTINVQVWDKSMVSSVEKGITIANLGLTHATDGQLIRLPIPSLTEERRKELVKLAHKYGEETKISLRNIRRDGIEELKKLEKDNIIVKDEYHNLSEQIQKLTDEYSSKVDSAIKQKEQEIMTV
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Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. {ECO:0000255|HAMAP-Rule:MF_00040}.
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Q9ZE09
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GATC_RICPR
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Glutamyl-tRNA(Gln) amidotransferase subunit C (Glu-ADT subunit C) (EC 6.3.5.-)
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MITKEEAQKIAKLARLKFEKDIVEKFSTQLSTIMNMINILNEIDCKDIEPLTSVSNMNARMREDTVTSSDLSNKLFDNVSGNSAKLAKEVKYFITPKVVE
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Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
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Q9ZE10
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GATA_RICPR
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Glutamyl-tRNA(Gln) amidotransferase subunit A (Glu-ADT subunit A) (EC 6.3.5.7)
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MTELNKLTVAESVKGLKNKDFTSKELVNAYIKQIEKYKNLNAYVTETFDLALKQAEAADQNYGQNKARTLEGIPFAVKDLFCTKGIRTTACSNILKNFIPHYESSVTQNIFDKGGVILGKTNMDEFAMGSANITSCFGNVISPWKANDDNSDLVPGGSSGGSAAAVSAFMASAALGSDTGGSVRQPASFTGLVGFKPTYGRCSRYGMVSFASSLDQAGIFTRSVLDSSIMLEAMMGFDEKDSTSINAQVPELQSAIGSSMKNMKIGVPLSLGEGGIIEHDIMKMWHDTIELLKNAGAEIVDITLPHAKYGVAVYYVIAPAEAASNLSRYDGVRYGLRVECENMTLDEMYEMTRSAGFGEEVKRRIMLGTYVLSSHCMDAYYFKAQKVRRLVANDFNNAFAKVNAILLPTAPSAAFKIGKKQNDPTIMYLNDLFTIPASLAGLPCASVPAGLSARGLPLGMQIIGKQLDEYNVLKVASTIETGVKHIKFEPAGF
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Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) (By similarity).
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Q9ZE11
|
GATB_RICPR
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT subunit B) (EC 6.3.5.-)
|
MEYIEGNTGKWEYVIGLEIHAQISSKSKLFSGSSTLFAASPNSQVSYVDAAMPGMLPVLNKHCVYQAIKTGLVLKAKINKYSVFDRKNYFYADLPQGYQISQFYYPIVQDGMIEIPTSTGDLKTIRINRLHLEQDAGKSIHDQSPYYSLIDLNRAGIGLMEIVTEPDISSPEEAAEFVKKLRNLLRYIGSCDGDMEKGSMRCDANISVRRIGEALGTRCEIKNINSIRNIIKAIEFEAKRQVDLLESGETIIQETRLFNVDSCETKTMRLKEEALDYRYFPDPDLLPLIIPDELINELKASLPELPDQKIEKYIKKFGLSQYDAGIIVSDEAVAEYFEKAANECNPKMLTNWLITELFGQLNKASIGIRECKITPSDFAKLIKLIEHDTISGKIAKTVFEIMFETGKAPDKIVEEKRLVQISDNKILNTVIDEVIAENSKSVKCYKSGKDKLFGFFVGQVMKKTECKANPTLVNKLLKDKLDS
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Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
|
Q9ZE21
|
RL7_RICPR
|
Large ribosomal subunit protein bL12 (50S ribosomal protein L7/L12)
|
MADLAKIEEQLSSLTLMQAAELVKMLEEKWGVSAAAPITVASAGVAAPLAEAVTEKTEFEVVLTATGDKKVEVIKIVKDITGLGLIEAKKLVDEAPKSIKNNVKKAEAEEIKSKLEAAGAKVELK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. {ECO:0000255|HAMAP-Rule:MF_00368}.
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Q9ZE22
|
RL10_RICPR
|
Large ribosomal subunit protein uL10 (50S ribosomal protein L10)
|
MLRSEKPVAVEDIVNIYKESPSVIITHYHGLTVSQVSSLREELKSKEAGFKVVKNTLAKIAAKQTGLDSITNLFAGPTAIVYSKEPVEMARLVVNFANSNDNLKIIGGIVDNHILDAYSIKELSKLPSLHELRGKIVGLLQAPATKVVGVLQATSSSIARVIHAHAIKH
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
Q9ZE23
|
RL1_RICPR
|
Large ribosomal subunit protein uL1 (50S ribosomal protein L1)
|
MSNKDICVKISGSKKIREAREKVKSDTLYNLTNAVAQLKSASYVKFDPTLEIVMKLGIDPRHSDQIVRGVVNLPAGTGKTIRVAVICKEEREEEAKSAGADLVGSINIIDEIKAGQINFDVCIATPDMMSMISSVARILGPKGLMPNPKLGTVTLDIKNAIKNAKSGQVEYRAEKAGIIHAGLGKLSFSDQDLLKNLNAFIGAVIKAKPVGLKGNYLKAIYLSSTMGASVQIDLTSIS
|
Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. {ECO:0000255|HAMAP-Rule:MF_01318}. Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. {ECO:0000255|HAMAP-Rule:MF_01318}.
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Q9ZE24
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RL11_RICPR
|
Large ribosomal subunit protein uL11 (50S ribosomal protein L11)
|
MSKKAIKGYINLIIPAAGATPAPPIGPALGQRKVNIAAFCKDFNDATNGMEKGVPLPTVITVYEDSSFSFKVKTPPASYFLKKYAKITKGSSATKKEAMVGKVTIDDCREIAKLKISDLNTKNIEAATKIICGSAASMGLEVVGN
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Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. {ECO:0000255|HAMAP-Rule:MF_00736}.
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Q9ZE27
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APBC_RICPR
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Iron-sulfur cluster carrier protein
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MANLHQQQIIDKIQNITFKDGTFLNEVISDIIIKGNNIGFSIDISGKNKLEAEEIRLKAINKLNNIKEVNKITIVFTQSKTIDKKAQKPKHFVENVKKIILVASGKGGVGKSTISALIAQQLSLENYRVGIVDADIYGPSIPHIFGINGIPKTVEGRIVPILAQNIQIISIGFFVKAHSAIIYRGPMASKIIYQLLSNTRWNNLDYLIIDMPPGTGDIHLSIIENYHLDGVIVVTTQQKISEIDVIRSIDLYRKLGLPILGIIENMIYMLESDHCGYLSKKYHIPLIAQIPIMPQIANACDKSLPLTNLLTLPLEKYL
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Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040}.
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Q9ZE34
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SECF_RICPR
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Protein translocase subunit SecF
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MQIYPLRFVPNKIDFDFMNFKKVSYSFSIILSLISLIWISIYKFNFGIDFVGGIVIEVRLDQAPDLPKMRAVLSALEIGEVVLQNFGSERDLSIRFGSSSEENLMKNIDIIKTSLRNNFPYNFEYRKVDFVGPQVGRQLIEAGAMAMLFSFLAIMVYIGVRFEWYFGFGILIALVHDVILALGFMSMTKLDFNLSTIAAVLTIIGYSVNDSVVIYDRIRENLRKYHKKNITEIINLSINETLSRTILTVITTLLANLALILFGGKAIHSFSVLVFFGIIAGTYSSIFISAPILTMFANRKFNKKVITQGKG
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Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. {ECO:0000255|HAMAP-Rule:MF_01464}.
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Q9ZE36
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RL19_RICPR
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Large ribosomal subunit protein bL19 (50S ribosomal protein L19)
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MNIIDNFEQENIAKLTANKKIPDFEAGDTVKVTVKIIDKAIEKDGKEKLTERFQAYEGVVIAKRNRGITSSFLVRKISHGEGVERRFMTYSPIVHSIDVVKYGVVRRAKLYYLRHRNGKAARIREKLISRAKPKTAIS
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This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
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Q9ZE37
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TRMD_RICPR
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tRNA (guanine-N(1)-)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase)
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MSILHVTILTVFPEMFPGTLGYSLAGQALHNNIWSYNIINIRDFGLTKHKNVDDKAYGGGDGLIMRPDVLGNAIENALSLNHNAKIYYPSPRGCVFTQSFAKEMLKNKNLIFLCGRYEGIDERVIAEYNVTEVSVGDYILSGGEIPTLTILDCLIRLLPGVLINQNTLSSESFEKDGEFQGGLECDLYTRPKIWRGRAVPSILLSGNHRLINNWRKEQSHMITKLRRPELLKDL
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Specifically methylates guanosine-37 in various tRNAs.
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Q9ZE46
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ENGB_RICPR
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Probable GTP-binding protein EngB
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MINNGKALNNKKSIDYSKLFRHQAKFVAGAIHINQIPDFSLPEIVFVGKSNVGKSSIINTICNNKSLAKVSNTPGRTRQINFFNIVDKLIIVDLPGYGFANVPISVKEQWEGLITYYLRNSHNLMLVNLLIDSRRGIKENDKKVAELLLANKREFQIIFTKSDKVTDRENLNYEAQNFLATLNYLCNVIYVSSRNKEGMRELKASFAQCIKHQR
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Necessary for normal cell division and for the maintenance of normal septation. {ECO:0000255|HAMAP-Rule:MF_00321}.
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Q9ZE47
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RL31_RICPR
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Large ribosomal subunit protein bL31 (50S ribosomal protein L31)
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MKNGIHPEYKKLLIKVGSNIFETMSTHPIGEILMDVDFRKHPAWNKDSGNVVNQSNKSVSDFNKRFAGLSFDSKKEAS
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Binds the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00501}.
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Q9ZE60
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EFTS_RICPR
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Elongation factor Ts (EF-Ts)
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MSEINISAVVVKELREKTGAGMMDCKKALIETSGNFEEAIDFLRKKGLAAAVKKSGRIASEGLTAVKVDGLISAVIEVNSETDFVARNKQFQDLVKDIVNLAIIAQNIDTLKISKMQSGKSVEEEIIDNIAIIGENLTLRRMDILEISNGAIGSYVHNEVVPHLGKISVLVGLESNAKDKVKLEALAKQIAVHVAGNNPQSIDTLSLDKSLIEREKKVFFEKSKEEGKPNHIIEKMVEGRIRKFFSEVVLLHQNFLFEPKLTVAEVIKNAEQELSAEIKITKFIRYALGEGIEHAEKNFADEVAAITQC
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Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).
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Q9ZE68
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SECG_RICPR
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Protein-export membrane protein SecG
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MIDIFLFVHITISILLIIVILMQRSGSGGISGISGDNNMGVVSAKTVGNFLSKSTIILTTLFLINAIVLANLSAKKQSDLVSKINEIEENQADNSLPIAK
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Involved in protein export. Participates in an early event of protein translocation (By similarity).
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Q9ZE76
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SECB_RICPR
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Protein-export protein SecB
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MSTINTDTSEAMPHISVNAQYIKDLSLENPSAPSSLAALDQRPQIDLSLDINITNLSEENFYEVELNIEAIARNEKYKLFQIELKYAGVFNLINIDSEQHPILLSVHCPAMIFPFARKIIASCTQDAGFQPLMIDPIDFGALYHKKMSEHQN
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One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. {ECO:0000255|HAMAP-Rule:MF_00821}.
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Q9ZE87
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PARB_RICPR
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Probable chromosome-partitioning protein ParB
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MVKNKGLGRGLSSLLGEEVLPIESEIVQIINIDKIKPNENQPRKHFEYNKIKELADSILNNGLLQPIIIDNNFQIIVGERRWRACKLAKVLEIPVIIKNFDTRESMEVALIENIQRTDLTVMEEARGFKYLVENFNYTVEKLAERLGKSRSHIANLLRLNNLPQSIQDKLNENILSMGHARCLINHEYAEEIADHIINHDLNVRQTEALVRQWHKNEYKKSSNNNNKVDKLCVKDNVIDNDLELLVKALSKKFGIKITIDNCRLGGKLMFHYKNLEELDLILSKLN
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Involved in chromosome partition. Localize to both poles of the predivisional cell following completion of DNA replication. Binds to the DNA origin of replication (By similarity).
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Q9ZE89
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RSMG_RICPR
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Ribosomal RNA small subunit methyltransferase G (EC 2.1.1.170) (16S rRNA 7-methylguanosine methyltransferase) (16S rRNA m7G methyltransferase)
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MKVQSEIIEKLEIFQNLIKKWNKSINLISDNTIPNFWQRHILDSLQLMQYISNKEIHLIDIGSGAGFPGIVLSIAGVTKVSLIEADLRKCIFLAKASKISNNSIQIINQRIEKIEIDCSILTCRAFSNLNTIFNYTQNISVREKFLLLKGKSYLTEIVEAKERWSFDYLIHQSITCGSGKILEINNLTKII
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Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}.
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Q9ZE90
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MNMG_RICPR
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tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG (Glucose-inhibited division protein A)
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MLKYGVIIIGGGHAGVEAAAASARLGVHTLLITLKPENLGEMSCNPAIGGIAKGTLVKEIDALDGLMGFVIDKSGIHYKMLNETRGPAVWGPRAQADRKLYKKVMYQILTNYRNLDILYAKVEDIQIKSSKVEAVILSNGSKIFCQKVVLTTGTFLSGFIHIGSIKMPAGRIYEEPSYGLSNTLKRLGFKIARLKTGTPPRIDGRTIDYSKTALQQGDQIPRPFSELTDVIDVPQINCFITKTTSETHDIIRENLDKSAMYSGQIEGIGPRYCPSIEDKIVKFSTKLEHRIFLEPEGLEDYTIYPNGISTSLPEEVQYKLIKTIPGLENAQVLRPGYAIEYDYVDPREINVTLETKKITGLYFAGQINGTTGYEEAAGQGIIAGINAALSVKDQAPFILTRATSYIGVMIDDLTTFGTVEPYRMFTSRSEYRLSLRADNADLRLTELGIKIGVITEKRKKFFTKKCKNIEKTKLLLNNLSLTTSKLAKMGIQVAQDGKYKTILDLFKIPSFNVEQAIKIFPILKKQNNNILQLLYIEAKYASYLTRQYADINLFQSEEIQLIPKNIDYFKIPSISLEIQEKLSYHKPATIGVARRISGITPASITAIIIYLKTKYSDESSK
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NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_00129}.
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