Datasets:
jonghyunlee
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UniProt_function_text_descriptions

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2.44k
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35.2k
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11k
Q9ZL21
UVRC_HELPJ
UvrABC system protein C (Protein UvrC) (Excinuclease ABC subunit C)
MADLLSSLKNLSSSSGVYQYFDKNRQLLYIGKAKNLKKRIKSYFSVRNNEITPNPRTSLRVQMMVKQIAFLETILVENEQDALILENSLIKQLKPKYNILLRDDKTYPYIYMDFSIDFPIPLITRKILKQPGVKYFGPFTSGAKDILDSLYELLPLVQKKNCIKDKKACMFYQIERCKAPCEDKITKEEYLKIAKECLEMIENKDRLIKELELKMERLSSNLRFEEALIYRDRIAKIQKIAPFTCMDLAKLYDLDIFAFYGGNNKAVLVKMFMRGGKIISSAFEKIHSLNGFDTDEAMKQAIINHYQSHLPLMPEQILLSACSNETLKELQEFISHQYSKKIALSIPKKGDKLALIEIAMKNAQEIFSQEKTSNEDRILEEARSLFNLECVPYRVEIFDTSHHSNSQCVGGMVVYENNAFQKDSYRRYHLKGSNEYDQMSELLTRRALDFAKEPPPNLWVIDGGRAQLNIALEILKSSGSFVEVIAISKEKRDSKAYRSKGGAKDIIHTISHTFKLLPSDKRLQWVQKLRDESHRYAINFHRSTKLKNMKQIALLKEKGIGEASVKKLLDYFGSFEAIEKASDQEKNAVLKKRK
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}.
Q9ZL36
ACPS_HELPJ
Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS)
MIGIDIVSIARIEKCVKRFEMRFLERFLSPSEIVLCKDKSSSIAGFFALKEACSKALQVGIGKELSFLDMRISKSPKNAPLITLSKEKMDYFNIQSLSASISHDAGFAIAVVMVSSSNL
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP-Rule:MF_00101}.
Q9ZL45
MOG_HELPJ
Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75)
MQTIHIGVLSASDRASKGVYEDLSGKAIQEVLSEYLLNPLEFHYEIVADERDLIEKSLIKMCDEYQCDLVVTTGGTGPALRDITPEATKKVCQKMLPGFGELMRMTSLKYVPTAILSRQSAGIRNKSLIINLPGKPKSIRECLEAVFPAIPYCVDLILGNYMQVNEKNIQAFRPKQ
Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor.
Q9ZL50
CLPP_HELPJ
ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Endopeptidase Clp)
MGYIPYVIENTERGERSYDIYSRLLKDRIVLLSGEINDSVASSIVAQLLFLEAEDPEKDIGLYINSPGGVITSGLSIYDTMNFIRPDVSTICIGQAASMGAFLLSCGAKGKRFSLPHSRIMIHQPLGGAQGQASDIEIISNEILRLKGLMNSILAQNSGQSLEQIAKDTDRDFYMSAKEAKEYGLIDKVLQKNVK
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}.
Q9ZL51
DEF_HELPJ
Peptide deformylase (PDF) (EC 3.5.1.88) (Polypeptide deformylase)
MALLEIIHYPSKILRTISKEVVSFDSKLHQQLDDMHETMIASEGIGLAAIQVGLPLRMLIINLPQEDGVQHKEDCLEIINPKWIETKGSIMYREGCLSVPGFYEEVERFEKVKIEYQNRFAEVKILEASELLAVAIQHEIDHLNGVLFVDKLSILKRKKFEKELKELQKKQKHK
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).
Q9ZL58
LOLA_HELPJ
Outer-membrane lipoprotein carrier protein
MKAFLKICMVLIFVGVAHAKNPLTLSKEEEVLQNLQSFSAHFKQVLKNEKPLVYYGVLKAKAPNWALWVYEKPLKKEIYMNDKEVVVYEPNLFQATITPLKDKTDFFTILKQLKKQTDGSFKTTINKTTYRLVFKDGKPFSLEFKDDMNNLVTITFSQAEINPKIPNEIFVFNPKDENIDIVRQ
Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane) (By similarity).
Q9ZL73
FLHB_HELPJ
Flagellar biosynthetic protein FlhB
MAEEEKTELPSAKKIQKAREEGNVPKSMEVVGFLGLLAGLMSIFVFFIWWVDGFSEMYRHVLKDFSLDFSKESVQELFNQLAKDTFLLLLPVLIILMVVAFLSNVLQFGWLFAPKVIEPKFSKINPINGVKNLFSLKKILDGSLITLKVFLAFFLGFFIFSLFLGELNHAALLNLQGQLLWFKSKALWLISSLLFLFFVLAFVDLIIKRRQYTNSLKMTKQEVKDEYKQQEGNPEIKAKIRQMMVKNATNKMMQEIPKSNVVVTNPTHYAVALKFDEEHPVPVVVAKGTDYLAIRIKGIAREHDIEIIENKTLARELYRDVKLNATIPEELFEAVAIVFAQVAKLEQERQKQKIIKPL
Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin (By similarity).
Q9ZL83
RNY_HELPJ
Ribonuclease Y (RNase Y) (EC 3.1.-.-)
MSSGLIYISLEVLVACLITALIMYYVMKKIYYARGQAILKGASAKAKLMEFQAKSFVEAEEMRMKSQECKLQQQYENKNLQLQTHFDKKEAHLKHLEAQHKEFVRDEKRYLEKEKKELEKERQILEQERENFKKQRAICKEAQAKALDAMLNYMAYTKDEIKSMILEQLEEELEAQKSALIRRYEKEAKEEGKKKSYAILAEATARFAGDYATENLTSRIALPCSDYVGRVIGKDGKNIEAFKKISGVDIEFSEDSSELCLSSFNIYRREVASETIKILIEDGRIQPNRIEEVYHRVARNMEKELLSEGESVVLELELGTMEDELKILIGKMRYRFSFGQNALQHSKEVALLAGLIAEQLGGDKKLARRAGILHDIGKALTQELGRDHVNLGVEVCKRHKEDPVVINAIYAHHGHEEIMSVECASVCAADALSAGRPGARRKSDEEYAKRMQALEEIALEFDGVEKAYAMESGRELRVIVKSNQVRDNQVPIIARKIAKRIEESTQYVGEVGVQVVRENRFKTTATLKQ
Endoribonuclease that initiates mRNA decay. {ECO:0000255|HAMAP-Rule:MF_00335}.
Q9ZL96
TRMB_HELPJ
tRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.33) (tRNA (guanine(46)-N(7))-methyltransferase) (tRNA(m7G46)-methyltransferase)
MPHFLAKLDSKPLEYPLIRGDFCFHREFLSLKHPTKSCVHASFKNDVFLLQKIRRAGDFLIKSEKATPLKREILKQALRIYSQSFEVISHNLQENSKHASQKKALDLETFEDFIQKNQAPILIEIGFGSGRHLIELAKNNPTTTCLGIEIHTPSIAQALKQIELLDLKNLHILQGDGRLVLESMPNHRCEKIFVHFPVPWNEKKHRRVLSEKFLNEALRVLKPRGFLELRTDDSLCFEDSLKLALKNFQCEIEIKKNAQIPVVSKYEARWNKLKKDIYDLKIYSLGLDENPTQNHALDFSFDTITIDKESVGAILKTPKIIKEGYFVHVCNIYENKGDFLVELSMGDFDWPVRLFVLLAENQVFYLNKSPLKTLNNHKAHLLLQNILSQKELDERDHRSE
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057}.
Q9ZLB5
TILS_HELPJ
tRNA(Ile)-lysidine synthase (EC 6.3.4.19) (tRNA(Ile)-2-lysyl-cytidine synthase) (tRNA(Ile)-lysidine synthetase)
MTARDFKNYLEPLREGKNLLGFSGGLDSTCLFHLLVGENIAFDIALVDYSTQKQRLEIIQHAQKLAQTHHKKCYIHYAPKIARNFEMQARKVRYDFFETLIKEHSYKHLILAHHLNDRLEWFLMQLSKGAGLNTLLSFQAYEKRESYAIVRPLLYTPKDTLKTLAKDQKFFEDDSNSSLKFKRNCFRKHYANALMQHYSKGIIQSFKFLDKEKERLYPLIPVSQMHGITFFKHSHNALFMVDKILKKKGYVLSFLQKEEIKHHFFSLEIAQKFIIEKDKEHVFIAFKPQKTLSMPKDFKDRARRLDIPKRLRPVLYAEFLKQPTHDFLTRFKQSLMDL
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. {ECO:0000255|HAMAP-Rule:MF_01161}.
Q9ZLB6
DUS_HELPJ
Probable tRNA-dihydrouridine synthase (EC 1.3.1.-)
MDFKNKKWLFLAPLAGYTDLPFRSVVKKFGVDVTTSEMVSSHSLVYAFDKTSKMLEKSPLEDHFMAQISGSKESVVKEAVEKINALDHVSGIDFNCGCPAPKVANHGNGSGLLKDLNHLVEILKVIRENTNKKITSVKVRLGFEKKIPKEIAHALNDAPVDYVVVHGRTRSDRYQKDKIDYESIALMKKILKKPVIANGEIDSVKKAFEVLQITQADGLMIGRATLRAPWIFWQIRNNTTELPAVVKKDLVLEHFDKMVEFYGDRGVIMFRKNLHAYAKGEMQASAFRNCVNTLTEIKSMRESIEEFFNQEMLQSEVPLWVELNQKSV
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Q9ZLC0
DCUA_HELPJ
C4-dicarboxylate transporter DcuA
MVDAFFQIIVLLFSLFLGARLGGLGVGYAGGLGVLILCLFLGLNPGKIPFDVILIIMAVISAISAMQKAGGLDYLVQIAEKILRKHPKQINYLAPSVAYFLTILAGTGHTVFSLIPVIVEVSQSQNIKPKAPLSLAVVSSQVAITASPVSAAVVFMSGILEPLGADYLTLLMVWIPTTFLACMLTAFVMGFTDLKLDSDPNYLERLKAGKISPPMMKKEKETSKSAKLSLWIFIGGVVAIVFYASAISKNIALISPVILGRDYAIVSFMLSVATLIAIFCKINANEIAHSSVFKSGMQACVCVLGVAWLGDTFVSNHIDEIKRYASFLIADYPFLLAVALFLASMLLYSQAATSKALIPSVITALGISANHTEHLYIIVASFASVSALFVLPTYPTLLGAIAMDHTGTTKMGRYVFDHAFLIPGVLVVFLSVALGFVVAPLVL
Responsible for the transport of C4-dicarboxylates.
Q9ZLC8
RP54_HELPJ
RNA polymerase sigma-54 factor
MAILRANLSPKNKLNATLKGWLPILQSELEDLEEVLKQNALDNPLIKIENKRIKNFSDRFNTKKSSDHLENCATASKSLFETLESQIIPPLFPTETSQKIAMDIISGLNNEGYFEENIEERAKVLGVESEVYEKVRKRFSYLNPAGIGAKDVKEGFLFQLDGRELDNNELYEETRKIILNLEKHHEFSKDFYYEKALKILKSFKNPPAIEFLEKEIEVIPELFILEVDNEMIVRLNDESYPTISLEENRFKDSDYLKEKLKEAKDLIDALNLRKATIYKIGLMLLEYQYDFFKGKELRPLKLLDLANEFNHSVSTISRAISNKYLACERGVFPIKHFFSIALDNSETSNAVIKDYLLELIKNEDKKEPLSDAKILELIEEKFHLKMVRRTITKYRQLLNIASSSERKRLYLMRA
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
Q9ZLD4
RSMH_HELPJ
Ribosomal RNA small subunit methyltransferase H (EC 2.1.1.199) (16S rRNA m(4)C1402 methyltransferase) (rRNA (cytosine-N(4)-)-methyltransferase RsmH)
MQEIENLHQSVLLQEVLQAFTPLEEGILIDCTLGLGGHSKAILSQKPHLKLIGIDKDKFAQEIAKERLKEFEGRYNLLSGGFAKRFKEALEIHGERIKGVLVDLGVSSLQLDDDNRGFNFRSHALDMRMDLESELNAQKVINSYPVVALEKIFRDYGEIKEYKKIAHKIAERRAKKPFKDAKDLSEFLSSLSKNKKIHPATLVFQAVRIEVNSELEELKEFLQCARNLKEAILCVISFHSLEDALVKNAFKDYAKNCICDPSSFKCACSNNHALGAILTKKPITPSPEEIKNNRRSRSAKMRVFQFKP
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01007}.
Q9ZLF3
FEOB_HELPJ
Fe(2+) transporter FeoB (Ferrous iron transport protein B)
MKEIIVALVGQPNVGKSSLINALSNAHLKVGNFAGVTVDKMEVSLIHKDHQITIIDLPGTYALNDFTTEEKVTKDFLEKGQYDLILNVVDSTNLERNLALSAQLLDTNKKMLLALNMWDEAKKEGININTEKLSQELGVVCVPTSARSKEDRLNTELLLDEIVRLYSQNTTNNENIKVPSQSFKESLKYSQSAQRIAKSVISENKQNASFEHTYKIDKILMHQRYGIFIFLGFMFIIFSLSFLIGGGVQKALEEGFKILSDSIKENVANEDLASLVGDGIIGGVGATVSFLPLIVVLYFGISLLETTGYMSRVAFLLDGILHKFGLHGKSFIPLITGFGCSVPAYMATRTLQNYNERLITLFVIGFMSCSARLPIYVLFVGSFFPSSSAGFVLFCIYILGAVVALVMAKLLKLSVFKGQTESFIMEMPKYRFPSWRMVYFSIYTKSLSYLKKAGTYILVGAILIWFMSQYPKNDAAMKTYKQESLLVQKNANLSSEAKEEKLKELKTELDKKNLKNSVVGRGGAYLEKVFNPMDFDWRLSVSLVTGFMAKEVVVSTLGVLFSLGDQNEKSDAFREIIRKEVSVPSGIAFIVFVMFYIPCFAATITFGREAGGIKFVAYLFIFTTVVAYAFSLIAFYATQILV
Probable transporter of an ATP-driven Fe(2+) uptake system.
Q9ZLH6
GATB_HELPJ
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT subunit B) (EC 6.3.5.-)
MPFEAVIGLEVHVQLNTKTKIFCSCSTSFGETPNSNTCPVCLGLPGALPVLNKEVVKKAIQLGTAIEAHINQYSIFARKNYFYPDLPKAYQISQFEVPIVSDGKLEIDTKEGAKIVRIERAHMEEDAGKNIHEGSYSLVDLNRACTPLLEIVSKPDMKNSEEAIAYLKKLHAIVRFIGISDANMQEGNFRCDANVSIRPKGDEKLYTRVEIKNLNSFRFIAKAIEYEIERQSVAWENGRYNEEVVQETRLFDTAKGITLSMRNKEESADYRYFKDPDLYPVFIDEKLLKEAQKINELPGAKKIRYMKDFNLKEDDANLLVSDPLLAEYFESMLNLGVKAKTSVTWLCVELLGRLKAEVTLENCGISAHALGALAKRIDEGKISGKSAKDVLDRLLEEQGGDVDTLIEQMGLSQVNDTEAIVKVIEEVLKNNADKVLEYKSGKDKLFGFFVGQAMKNLKGANPSVVNAILKEKLD
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).
Q9ZLQ9
APT_HELPJ
Adenine phosphoribosyltransferase (APRT) (EC 2.4.2.7)
MNEMLKEELLQSIREVKDYPKKGILFKDITTLLNYPKLFNKLIDALKKRYLALNIDFIVGIEARGFILGSAFAYALGVGFVPVRKKGKLPAHTLSQSYSLEYGSDSIEIHSDAFRGIKGVRVVLVDDLLATGGTALASLELIKALQAECIEACFLIGLKELPGIQLLEEHVKTFCLLEC
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. {ECO:0000255|HAMAP-Rule:MF_00004}.
Q9ZLS1
ACP_HELPJ
Acyl carrier protein (ACP)
MALFEDIQAVIAEQLNVDAAQVTPEAEFVKDLGADSLDVVELIMALEEKFNIEIPDEQAEKIVNVGDVVKYIEDNKLA
Carrier of the growing fatty acid chain in fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}.
Q9ZLS8
RSMI_HELPJ
Ribosomal RNA small subunit methyltransferase I (EC 2.1.1.198) (16S rRNA 2'-O-ribose C1402 methyltransferase) (rRNA (cytidine-2'-O-)-methyltransferase RsmI)
MLYFLPTPIGNLADITLRTLEVLERCEVFLCEDTRVSKRLLHLLAKNPIISHSFPNIAAKKREFIAFHSHNDQEFLNQIEPSFFDKEIAVMSDAGMPSLSDPGMSLVAYALKHNLQYDVLPGANALTTAFCASGFLEGRFFYAGFLPHKSKERRLRIIKILNALAYLEEKTPVVFYESPHRLLETLRDLNDLAQGMHLFAAKELTKLHQQYYLGEISQIMTQLQKSNIQGEWVLVLLNEKKIEPSMGLSALLELDLPPKIKAKMEAAMTQKNAKELYFQRLLEEKKQCD
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}.
Q9ZLT1
CAGA_HELPJ
Cytotoxicity-associated immunodominant antigen (120 kDa protein) (CAG pathogenicity island protein 26)
MTNEAINQQPQTEAAFNPQQFINNLQVAFIKVDNVVASFDPNQKPIVDKNDRDNRQAFEKISQLREEFANKAIKNPTKKNQYFSSFISKSNDLIDKDNLIDTGSSIKSFQKFGTQRYQIFMNWVSHQNDPSKINTQKIRGFMENIIQPPISDDKEKAEFLRSAKQAFAGIIIGNQIRSDQKFMGVFDESLKERQEAEKNGEPNGDPTGGDWLDIFLSFVFNKKQSSDLKETLNQEPVPHVQPDVATTTTDIQSLPPEARDLLDERGNFSKFTLGDMNMLDVEGVADIDPNYKFNQLLIHNNALSSVLMGSHNGIEPEKVSLLYGNNGGPEARHDWNATVGYKNQRGDNVATLINVHMKNGSGLVIAGGEKGINNPSFYLYKEDQLTGSQRALSQEEIQNKVDFMEFLAQNNAKLDNLSKKEKEKFQNEIEDFQKDSKAYLDALGNDHIAFVSKKDKKHLALVAEFGNGELSYTLKDYGKKADKALDREAKTTLQGSLKHDGVMFVDYSNFKYTNASKSPDKGVGATNGVSHLEAGFSKVAVFNLPNLNNLAITSVVRQDLEDKLIAKGLSPQEANKLVKDFLSSNKELVGKALNFNKAVAEAKNTGNYDEVKQAQKDLEKSLKKRERLEKDVAKNLESKSGNKNKMEAKSQANSQKDEIFALINKEANRDARAIAYAQNLKGIKRELSDKLENINKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSIKDVIINQKITDKVDNLNQAVSVAKATGDFSGVEQALADLKNFSKEQLAQQAQKNEDFNTGKNSALYQSVKNGVNGTLVGNGLSKAEATTLSKNFSDIKKELNAKLGNFNNNNNNGLENSTEPIYTQVAKKVKAKIDRLDQIASGLGDVGQAASFLLKRHDKVDDLSKVGLSANHEPIYATIDDLGGPFPLKRHDKVDDLSKVGLSREQKLTQKIDNLNQAVSEAKASHFDNLDQMIDKLKDSTKKNVVNLYVESAKKVPTSLSAKLDNYATNSHTRINSNVKNGTINEKATGMLTQKNSEWLKLVNDKIVAHNVGSAPLSAYDKIGFNQKNMKDYSDSFKFSTRLSNAVKDIKSGFVQFLTNIFSMGSYSLMKASVEHGVKNTNTKGGFQKS
May be necessary for the transcription, folding, export, or function of the cytotoxin.
Q9ZLW1
HSLU_HELPJ
ATP-dependent protease ATPase subunit HslU (Unfoldase HslU)
MSKLNMTPREIVAYLDEYIIEQKEAKKFIAIALRNRYRRLQLEKSLQEEITPKNILMIGSTGVGKTEIARRMAKIMKLPFVKVEASKYTEVGFVGRDVESMVRDLVNNSVLLVENEHKERLKDKIEEAVVEKIAKKLLPPLPSGVSEEKKQEYANSLLKMQQRIAQGELDSREIEIEVRKKSIEIDSNVPPEILRVQENLIKVFHKEQDKVKKTLSVKEAKEALKAEISDTLLDGEAIKMEGLKRAESSGVIFIDEIDKIAVSSKEGSRQDPSKEGVQRDLLPIVEGSVVNTKYGSIKTEHILFIAAGAFHLSKPSDLIPELQGRFPLRVELENLTEEIMYMILTQTKTSIIKQYQALLKVEGVEIAFEDDAIKELAKLSYNANQKSEDIGARRLHTTIEKVLEDISFEAEDYSGQSVTITKELVQSKLGDLVADENLVKYIL
ATPase subunit of a proteasome-like degradation complex this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. {ECO:0000255|HAMAP-Rule:MF_00249}.
Q9ZLW3
RL9_HELPJ
Large ribosomal subunit protein bL9 (50S ribosomal protein L9)
MKVLLLEDVKNLGKAGEVCEVKDGYGNNFLIANQKAKLATNEVINKYKAEVKKKAEKEALEKAQKLQMVETLQTITLTIHKKVGANGSLFGAITKEEITERLKEQHASLNLDKKDIELKHPIKSTGIYEIEVKLGSGIAGVFKIDVVAE
Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00503}.
Q9ZLW8
PGBA_HELPJ
Plasminogen-binding protein PgbA
MLRLLIGLLLMSFISLQSASWQEPLRVSIEFVDLPKKIIRFPAHDLKVGEFGFVVTKLSDYEIVNSEVVIIAVENGVATAKFKAFESMKQSHLPTPRMVAKKGDLVYFRQFNNQAFLIAPNDELYEQIRATNTDINFISSDLLVTFLNGFDPKIANLRKACNVYSVGVIYIVTTNTLNILSCESFEILEKRELDTSGVTKTSTPFFSRVEGIDAGTLGKLFSGSQSKNYFAYYDALVKKEKRKEVRIEKKEERIDARENKREIKQEAIKEPKKANQGTENAPTLEEKNYQKAERKFDAKEERRRSRDERKKTKATKKAMEFEEREKEHDERDEKETEERRKALEMDKGNEKVNAKENEREINQESANEPSSENNATLKDTENTSVLKESAAKKEAPKPSSKEEKRRLKEEKKKAKAEQRAREFEQRAREHQERDEKELEERRKALEMNKK
Binds plasminogen, specifically, and in a concentration and lysine-dependent manner. Plasminogen is the precursor of plasmin, a serine protease that cleaves fibrin, fibronectin, laminin and vitronectin. Acquisition of plasminogen/plasmin could enable H.pylori to degrade host components (By similarity).
Q9ZLX4
DPO3B_HELPJ
Beta sliding clamp (Beta clamp) (Sliding clamp) (Beta-clamp processivity factor) (DNA polymerase III beta sliding clamp subunit) (DNA polymerase III subunit beta)
MKISVSKNDLENTLRYLQAFLDKKDASSIASHIHLEVIKEKLFLKASDSDIGLKSYISTQSTDKEGVGTINGKKFLDIISCLKDSNIVLETKDDSLVIKQNKSSFKLPMFDADEFPEFPVIDPKVSLEINAPFLVDAFKKIAPVIEQTSHKRELAGVLMQFNQKHQTLSVVGTDTKRLSYTQLEKISIHSTEEDISCILPKRALLEILKLFYENFSFKSDGMLAVVENETHAFFTKLIDGNYPDYQKILPKEYTSSFTLGKEEFKEGIKLCSSLSSTIKLTLEKNNALFESLDSEHSETAKTSVEIEKGLDIEKAFHLGVNAKFFLEALNALGTTQFVLKCNEPSSPFLIQEPLDEKQSHLNAKISTLMMPITL
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.
Q9ZLX8
YBGC_HELPJ
Acyl-CoA thioesterase YbgC (EC 3.1.2.-)
MRCRVYYEDTDSEGVVYHANYLKYCERARSEFFFKQNVLPENEEGVFVIRSIKADFFTPASLGQVLEIRTQIKELRKVFVVLFQEIYCIQNASLEPMKPFKVFASEIKFGFVNRSTYSPIAIPKLFKELLSAV
Thioesterase that may be involved in phospholipid metabolism. Displays acyl-CoA thioesterase activity with lauroyl-CoA (C12:0), myristoyl-CoA (C14:0), palmitoyl-CoA (C16:0), stearoyl-CoA (C18:0) and benzoyl-CoA, catalyzing the hydrolysis of the thioester bond. Has low activity with butyryl-CoA and octanoyl-CoA (By similarity).
Q9ZM26
FUR_HELPJ
Ferric uptake regulation protein (Ferric uptake regulator)
MRRLETLESILERLRMSIKKNGLKNSKQREEVVSVLYRSGTHLSPEEITHSIRQKDKNTSISSVYRILNFLEKENFICVLETSKSGRRYEIAAKEHHDHIICLHCGKIIEFADPEIEHRQNEVVKKYQAKLISHDMKMFVWCKECQESDD
Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes.
Q9ZM34
FLHF_HELPJ
Flagellar biosynthesis protein FlhF (Flagella-associated GTP-binding protein)
MKFYTYSGETAAEALKIAQSHHGVDTLVFKTQEIRKKTLTSSGLYEIVVAVEEEENKKAPLIPESLYDEELNEEDVVMQLSSTVEEMRKLAGVSSNQRNYTFSKNKTLLEKDAPLEDTPLEANKQDALLQALKDEANHKKEREKREVKQEEEIKDINAQLSKIRDSLKLIQNMFWDEKNPNSVNIPQEFAEIYKLAKQSGMKSSHLDEIMQLSLELMPLRMRENSVTIKRYFREVLRKIILCRPEDLNLRQKRILMLVGPTGVGKTTTLAKLAARYSRMLAKKYKVGIITLDNYRIGALEQLSWYANKMKMSIEAVIDAKDFAKEIEALEYCDFILVDTTGHSQYDKEKIAGLKEFIDGGYNIDVSLVLSVTTKYEDMKDIYDSFGVLGIDTLIFTKLDESRGLGNLFSLVHESQKPISYLSVGQEVPMDLKVATNEYLVDCMLDGFSNPNKEQA
Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum (By similarity).
Q9ZM39
RS15_HELPJ
Small ribosomal subunit protein uS15 (30S ribosomal protein S15)
MALNLEKKQEIIKAFATKANDTGSCEVQVALLNERIKLLTEHLKTNPKDHSSRLGLLKLVAQRRNLLKYIKRTDHVRYVVLIEKLGIKDR
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}.
Q9ZM40
FLHA_HELPJ
Flagellar biosynthesis protein FlhA
MANERSKLAFKKTFPVFKRFLQSKDLALVVFVIAILAIIIVPLPPFVLDFLLTISIALSVLIILIGLYIDKPTDFSAFPTLLLIVTLYRLALNVATTRMILTQGYKGPSAVSDIITAFGEFSVSGNYVIGAIIFSILVLVNLLVVTNGSTRVTEVRARFALDAMPGKQMAIDADLNSGLIDDKEAKKRRAALSQEADFYGAMDGASKFVKGDAIASIIITLINIIGGFLVGVFQRDMSLSFSASTFTILTIGDGLVGQIPALIIATATGIVATRTTQNEEEDFASKLITQLTNKSKTLVIVGANLLLFATIPGLPTFSLAFVGTLFLFIAWLISREGKDGLLTKLENYLSQKFGLDLSEKPHSSKIKPHAPTTKTKTPEEIKREEEQAIDEVLKIEFLELALGYQLISLADMKQGGDLLERIRGIRKKIASDYGFLMPQIRIRDNLQLPPTHYEIKLKGIVIGEGMVMPDKFLAMNTGFVNREIEGIPTKEPAFGMDALWIDAKNKEEAIIQGYTIIDPSTVIATHTSELVKKYAEDFITKDEVKSLLERLAKDYPTIVEESKKIPTGAIRSVLQALLHEKIPIKDMLTILETITDIAPLVQNDVNILTEQVRARLSRVITNAFKSEDGRLKFLTFSTDSEQFLLNKLRENGTSKSLLLNVGELQKLIEGVSEEAMKVLQKGIAPVILIVEPNLRKALSNQMEQARIDVVVLSHAELDPNSNFEALGTIHINF
Involved in the export of flagellum proteins.
Q9ZM44
RIMP_HELPJ
Ribosome maturation factor RimP
MTKKIEEKIEGVIESLGYLLYDVSLVKENEQHVLRVSLKNPNGAVSLDICQQVSEIISPLLDVCDFIQDAYILEVSSMGLERTLKTPKHFKLSLGEKVEVKLINKESFQAVLKDANDLSADFELDNHAIKSVEYKDLKKVKTLFEW
Required for maturation of 30S ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_01077}.
Q9ZM45
RBFA_HELPJ
Ribosome-binding factor A
MNAHKERLESNLLELLQEALASLNDSELNSLSVTKVECSKGKHHALVFVLSSDHKILSKLKKAEGLIRQFVLQASGWFKCPKLSFVLDDSLEKQLRLDAIFNEIAKGKDND
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00003}.
Q9ZM46
IF2_HELPJ
Translation initiation factor IF-2
MSDMVDLKKFVTELGKTQKELKNVIEQAKDIGLELKTNFKMTPEQAGKLYKYIVDGIKEQIQANQPTKNPKQDNKDDLNTAATPKPLAKKASKTPKKEETKAQPKPKKTKEKKKEAPAPIIKKKEIEIVNTFENQTPLVENTPKAVSHSQIEKAKQKLQEIQKSREALNKLTQSNTNTTNNANSASNVSNAKKEISEVKKQEQEIKRHENIKRRTGFRVIKRNDETENETENSVTESKKPTQSAAAIFEDIKKEWQEKDKQETKKTKKPSKPKATPTAKNNKSHKIDFSDVRDFKGNDIYDDETDEILLFDLHEQDNLNKEEEEKEARQNINDRVRVQRKNPWMNEAGIKRQSKKKRVFRNDNSQKVIQSAIAIPEEVRVYEFAQKANLNLADVIKTLFNLGLMVTKNDFLDKDSIEILAEEFHLEISVQNTLEEFEVEEVLEGVKKERPPVVTIMGHVDHGKTSLLDKIRDKRVAHTEAGGITQHIGAYMVEKNNKWVSFIDTPGHEAFSQMRNRGAQVTDIAVIVIAADDGVKQQTIEALEHAKAANVPVIFAMNKMDKPNVNPDKLKAECAELGYNPVDWGGEHEFIPVSAKTGDGIDNLLETILIQADIMELKAIEEGSARAVVLEGSVEKGRGAVATVIVQSGTLSVGDSFFAETAFGKVRTMTDDQGKSIQNLKPSMVALITGLSEVPPAGSVLIGVENDSIARLQAQKRATYLRQKALSKSTKVSFDELSEMVANKELKNIPVIIKADTQGSLEAIKNSLLELNNEEVAIQVIHSGVGGITENDLSLVSSSEHAVILGFNIRPTGNVKNKAKEYNVSIKTYTVIYALIEGMRSLLLGLMSPIIEEEHTGQAEVRETFNIPKVGTIAGCVVSDGEIARGIKARLIRDGVVVHTGEILSLKRFKDDVKEVSKGYECGIMLDNYNEIKVGDVFETYKEIHKKRTL
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).
Q9ZM48
KHSE_HELPJ
Homoserine kinase (HK) (HSK) (EC 2.7.1.39)
MVVSVPATSANLGPGFDCLGLSLNLRNRFFIEPSNIHAVKLVGEGEGIPKFLTNNIFTKVFYEILKKHGNDGSFKFLLHNKVPITRGMGSSSAMIVGAVASAFAFLGFAFDRENILNTALIYENHPDNITPAVFGGYNAAFVEKKKVISLKTKIPSFLKAVMVIPNRVISTKQSRHLLPKRYSVQESVFNLSHASLMTMAIVQGKWDLLRCCSKDRMHQYKRMQTYPVLFAIQKLALENNALMSTLSGSGSSFFNMCYEEDAPKLKQVLSKKFPKFRVAVLDFDNDGVLIEKD
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. {ECO:0000255|HAMAP-Rule:MF_00384}.
Q9ZM51
MINC_HELPJ
Probable septum site-determining protein MinC
MLKTNQKNVHAFEIEKQEPEAVMEFLEKNHALLQYFLIIFKYDIESEVKAVLHKHQLLFLETNRALNGRYIKTTEKDANLLKQNSPNAIEPKTTIYERNIRSGEEIYSTNHLIFLGNIHNGAKIISEGSVSVYGVCEGAIVCFGEYLILKEVKSAQIVFQNKILSLKEVERLLVNKNIKIITKNDDILDIKEVL
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization (By similarity).
Q9ZM58
TATB_HELPJ
Sec-independent protein translocase protein TatB
MFGMGFFEILVVLIVAIIFLGPEKFPQAVVDIVKFFRAVKKTLNDAKDTLDKEINIEEIKKETLEYQKLFENKVESLKGVKIEELEDAKVTAENEIKSIQDLMQDYKRSLETNTIPNHLNEEVSNEEALNKEVSSDESPKEVQLTTDNNAKEHDKEKEHV
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. {ECO:0000255|HAMAP-Rule:MF_00237}.
Q9ZM59
TATC_HELPJ
Sec-independent protein translocase protein TatC
MFEDLKPHLQELRKRLMVSVGTILVAFLGCFHFWKNIFEFVKNSYKGTLIQLSPIEGVMVAVKISFSAAIVISMPIIFWQLWLFIAPGLYKNEKKVILPFVFFGSGMFLMGAAFSYYVVFPFIIEYLATFGSDVFAANISASSYVSFFTRLILGFGVAFELPVLAYFLAKVGLITDASLKAYFKYAIVVIFIVAAIITPPDVVSQIFMALPLVGLYGLSILIAKMVNPAPKDNENDHENDAKEHTKSES
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. {ECO:0000255|HAMAP-Rule:MF_00902}.
Q9ZM60
QUEA_HELPJ
S-adenosylmethionine:tRNA ribosyltransferase-isomerase (EC 2.4.99.17) (Queuosine biosynthesis protein QueA)
MKEFDLESYDYHLPKELIANYPVLPKEKAKLLVYERRSQTITHTTFEHVLDFFPKNALVVLNDTKVIKARLFGSKHAFLPSKTTEVFFHRFFKGNTALTQIKGKIKVGDKIFFDANYYAEVLELLHNGQRLIAFYDNQTPLNQENILKLLEQYGHMPLPPYIKRADESLDAHEYQSVFAKHIGAVAAPTASLHFSQNALEKLLKDFKHAFLTLHVGAGTFLSVETKDIREHQIHTEVLHIPKKSQEILQESQEVLCIGTTALRSVEYFKRLKNPNQESFECDIFLHLANPIQHVNHLLTNFHLPKSSLLMLVSAMIGLEKTKEIYKIAIEKKYRFYSYGDGMLIL
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}.
Q9ZM61
RSMG_HELPJ
Ribosomal RNA small subunit methyltransferase G (EC 2.1.1.170) (16S rRNA 7-methylguanosine methyltransferase) (16S rRNA m7G methyltransferase)
MNPLLQDYARILLEWNQTHNLSGARNLSELEPQITDALKPLEFVKDFKSCLDIGSGAGLPAIPLALEKPEAQFILLEPRVKRAAFLNYLKSVLPLNNIEIIKKRLEDYQNLLQVDLITSRAVASSSFLIEKSQRFLKDKGYFLFYKGEQLKNEIAYKTTECFMHQKRVYFYKSKESLC
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}.
Q9ZM64
CHEY1_HELPJ
Chemotaxis protein CheY1
MKLLVVDDSSTMRRIIKNTLSRLGYEDVLEAEHGVEAWEKLDANADTKVLITDWNMPEMNGLDLVKKVRADNRFKEIPIIMITTEGGKAEVITALKAGVNNYIVKPFTPQVLKEKLEVVLGTND
Chemotactic response regulator protein that modulates the rotation direction of bacterial flagellar motors. Plays an important role in the colonization and infection of Helicobacter pylori. Upon phosphorylation by CheA, interacts with the flagellar motor protein FliM to cause clockwise flagellar rotation and bacterial reversals, as opposed to straight swimming when CheY1 is not phosphorylated.
Q9ZM65
PRMA_HELPJ
Ribosomal protein L11 methyltransferase (L11 Mtase) (EC 2.1.1.-)
MLESMYYEFFFIFPKERELFESFLLDTTHLALEESSLENLKAFDDKETIEFVSQSSWRYFATHDPLKENLKEKPPHLKNFVILRSEKNLSDSLFPALEAFCLNLKQSLQSEFDFFYLSRNLASKDWLEAYKQAVLPVRCAKFYIHPSWHQKPSHAAIDDCIMIDPALAFGSGHHESTSMCLELLSSLDLKRKNALDVGCGSGILSIALKKQGVSALTACDTDSLAVEETLKNFSLNQIPLLAQDKVIYGSTQKIEGRFDIIVANLVADVIKSLYSEFVRLCNHTLILSGILETHLNSVLQIYYNGFEVLEQRQRNEWVALKLLKKQSIN
Methylates ribosomal protein L11. {ECO:0000255|HAMAP-Rule:MF_00735}.
Q9ZM70
COPP_HELPJ
COP-associated protein (Copper ion-binding protein)
MKVTFQVPSITCNHCVDKIEKFVGEIEGVSFIDASVEKKSVVVEFDTPATQDLIKEALLDAGQEVV
Part of a cation-transporting system which is associated with copper export out of the H.pylori cells.
Q9ZM74
NIXA_HELPJ
High-affinity nickel-transport protein NixA
MKLWFPYFLAIVFLHALGLALLFMANNASFYAAASMAYMLGAKHAFDADHIACIDNTIRKLTQQGKNAYGVGFYFSMGHSSVVILMTIISAFAIAWAKEHTPMLEEIGGVVGTLVSGLFLLIIGLLNAIILIDLLKIFKKSHSNESLSRQQNEEIERLLTSRGLLNRFFKPLFNFVSKSWHIYPVGFLFGLGFDTASEIALLALSSSAIKVSVVGMLSLPILFAAGMSLFDTLDGAFMLKAYDWAFKTPLRKIYYNISITALSVFIALFIGLIELFQVISEKLHLKFENRLLSTLQSLEFTDLGYYLVGLFVIAFLGSFFLWKIKFSKLES
High-affinity nickel intake protein. Imports nickel ions in an energy-dependent fashion. Necessary for the expression of catalytically active urease.
Q9ZMA5
YQGF_HELPJ
Putative pre-16S rRNA nuclease (EC 3.1.-.-)
MILACDVGLKRIGIAALLNGVILPLEAILRHNRNQASRDLSDLLRKKDIQVLVVGKPNESYADTHARIEHFIKLVDFKGEIVFINEDNSSVEAYENLEHLGKKNKRIATKDGRLDSLSACRILERYCQQVLKKG
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00651}.
Q9ZMA7
MINE_HELPJ
Cell division topological specificity factor
MSLFDFFKNKGSAATATDRLKLILAKERTLNLPYMEEMRKEIIAVIQKYTKSSDIHFKTLDGNQSVETIEVEIILPK
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell (By similarity).
Q9ZMA8
MIND_HELPJ
Septum site-determining protein MinD (Cell division inhibitor MinD)
MAIVVTITSGKGGVGKSTTTANLAIGLAESGKKVVAVDFDIGLRNLDMILGLENRIVYDVVDVMEKNCNLSQALITDKKTKNLSFLAASQSKDKNILDKEKVAILINALRADFDYILIDSPAGIESGFEHAILHADMALVVVTPEVSSLRDSDRVIGIIDAKSNRAKSGEEVHKHLIINRLKPELVANGEMISIEEVLKILCLPLIGIIPEDHHIISATNKGEPVIRTDCESAKAYQRITRRILGEEVEYVEFKAKRGFFSALKGIFS
ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity).
Q9ZMB1
LPXK_HELPJ
Tetraacyldisaccharide 4'-kinase (EC 2.7.1.130) (Lipid A 4'-kinase)
MKSDKPFLERYFYDPTLLQKGLIFALYPFSLIYQCIATIKRKTAKKHDFKIPIISIGNLIAGGSGKTPFILEIAPRYQEVAVVSRGYQRDSKGLVVVSVKGNILVPQKTAGDEAYLLALNLKQASVIVSEKRELGVLKALELGSKIVFLDDGFRFNFNQFNALLKPKVPPYYPFCLPSGLYRENIKSYKEAHLVITEDKDYQRITSITNPTKRMLLVTAIANPSRLDAFLPKEVVKKLYFRDHAPFDLKLLEKEFYQNNATSLLVTSKDLVKLQDCKLPLSVLDLKLEICPKVLEEIDRYILSYPCNIKEHL
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). {ECO:0000255|HAMAP-Rule:MF_00409}.
Q9ZMB3
FLGH_HELPJ
Flagellar L-ring protein (Basal body L-ring protein)
MKKALYLGAVAFGVVFSMASANEPNIDFNPPNYVEETPSKEFIPELNKLGSLFGQGERPLFADRRAMKPNDLITIVVSEKASANYSSSKDYKSASGGNSTPPRLTYNGLDERKKKEAEYLDDKNNYNFTKSSNNTNFKGGGSQKKSEDLEIVLSARIIKVLENGNYFIYGNKEVLVDGEKQILKVSGVIRPYDIERNNTIQSKFLADAKIEYTNLGHLSDSNKKKFAADAMETQMPY
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Q9ZMB7
KGUA_HELPJ
Guanylate kinase (EC 2.7.4.8) (GMP kinase)
MNNDFNLLILSGPSGAGKSTLTKYLQEKIPKTHFSLSTTTRKPREGEVDGLHYNFVSEEEFKQGIEKGQFLEWAIVHNHYYGTSKIPVEKALKEGKIVIFDIDVQGHEILKKHYPNACSVFISTKNQEILKERLLLRGTDSKETIEKRLINAYKEMQCLESFDYLIINEDLEKSKEIILSIAKTLVHRLKAFNFEKICKAWKNESL
Essential for recycling GMP and indirectly, cGMP.
Q9ZMB8
TATA_HELPJ
Sec-independent protein translocase protein TatA
MGGFTSIWHWVIVLLVIVLLFGAKKIPELAKGLGSGIKNFKKAVKDDEEEAKNELKTLDAQATQTKVHETSEIKSKQES
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. {ECO:0000255|HAMAP-Rule:MF_00236}.
Q9ZMD9
RL21_HELPJ
Large ribosomal subunit protein bL21 (50S ribosomal protein L21)
MSYAIFKHGGKQYKVVEGDIVLLDKMNKEPKALVELVEVLAVSKEGKLSCGKPFVNGAKIEAEVINEGRSKKVITFKKRRRKDSKTKRGFRRDFTRVRITKIVA
This protein binds to 23S rRNA in the presence of protein L20. {ECO:0000255|HAMAP-Rule:MF_01363}.
Q9ZME1
AMIE_HELPJ
Aliphatic amidase (EC 3.5.1.4) (Acylamide amidohydrolase)
MRHGDISSSPDTVGVAVVNYKMPRLHTKNEVLENCRNIAKVIGGVKQGLPGLDLIIFPEYSTHGIMYDRQEMFDTAASVPGEETAILAEACKKNKVWGVFSLTGEKHEQAKKNPYNTLILVNDKGEIVQKYRKILPWCPIECWYPGDKTYVVDGPKGLKVSLIICDDGNYPEIWRDCAMRGAELIVRCQGYMYPAKEQQIAIVKAMAWANQCYVAVANATGFDGVYSYFGHSSIIGFDGHTLGECGEEENGLQYAQLSVQQIRDARKYDQSQNQLFKLLHRGYSGVFASGDGDKGVAECPFEFYKTWVNDPKKAQENVEKFTRPSVGVAACPVGDLPTK
Catalyzes the hydrolysis of short-chain aliphatic amides to their corresponding organic acids with release of ammonia. {ECO:0000255|HAMAP-Rule:MF_01242}. Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates. {ECO:0000255|HAMAP-Rule:MF_01242}.
Q9ZMG9
PYRX_HELPJ
Probable dihydroorotase-like protein (Aspartate carbamoyltransferase 42 kDa non-catalytic chain)
MLLKNASFYDDEVLKRADIRLKDSLIIEIEENLSPTNNEEVVECEDLFVLPSFIDLSVTNLEGYENLKQKAFKGGVGLLNVFNGDQSGIKNIMAIKNNQLADIATLKNKGGEILIAPSDAFLELISHYAKSYNLPLLISLENSFEALNSGALAYELGQNFVDNAFENTRLVRFMEVSRALQIPVLLDKVNSIATLKLIKAFNDLGAKLQAQTPLSHLILDESVYEDYEPRFKIAPPLRDKEGQNALKEALKNNEIAMLTSLHASKNSNAQLFEESAFGCESIEDAFSVAYTFLVQKKVISFQQLIKVMTINQAKFLKLNAGEVKENQLANLMIVDLNAQTRVSNQNSPFYGLELYGEVQRMILKGQTTFIKENACKKS
Non-functional DHOase.
Q9ZMH1
CLPB_HELPJ
Chaperone protein ClpB
MNLFEKMTDQLHETLDSAIALALHHKNAEVTPMHMLFAMLNNSQGILIQALQKMPVDIEALKLSVQSELNKFAKVSQISKQNIQLNQALIQSLENAQGLMAKRGDSFIATDAYLLANMNLFESVLKPYLDTKELQKTLESLRKGRTIQDKNDDSNLESLEKFGIDLTQKALENKLDPVIGRDEEIIRMMQILIRKTKNNPILLGEPGVGKTAVVEGLAQRIVNKEVPKTLLNKRVVALDLSLLVAGAKYRGEFEERLKKVIEEVKKSANVILFIDEIHTIVGAGASEGGMDAANILKPALARGELHTIGATTLKEYRKYFEKDMALQRRFQPILLNEPSINEALQILRGLKETLETHHNITINDSALIASAKLSSRYITDRFLPDKAIDLIDEGAAQLKMQMESEPAKLSSVKRSIQRLEMEKQALEMENKESNHKRMQEILKELSDLKEEKIQLEAQFENEKEVFKEISRLKMEMEGLKKEAERFKRNGDYQQAAEIEYSKIPEKEKKEKELQHKWETMQQNGALLQNALTENNIAEIVSQWTHIPVQKMLQSEKNRVLNIESELQKRVVGQEKALKAIAKAIKRNKAGLSDSNKPIGSFLFLGPTGVGKTESAKALAQFLFDSDKNLIRIDMSEYMEKHAISRLIGAAPGYVGYEEGGQLTEAVRRKPYSVVLLDEVEKAHPDVFNLLLQVLDEGHLTDSKGVRVDFKNTILILTSNVASGALLEEDLSEADKQKAIKESLRQFFKPEFLNRLDEIISFNALDSHAIINIVGILFENVQKKALERGINITLDEKAKELIAEAGFDRFYGARPLKRALYEMVEDKLAELILEDKIKENDSVAFVVENNEIVPKIK
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Q9ZMH7
EX7L_HELPJ
Exodeoxyribonuclease 7 large subunit (EC 3.1.11.6) (Exodeoxyribonuclease VII large subunit) (Exonuclease VII large subunit)
MHVLSVSEINAQIKALLEATFLQVRVQGEVSNLTIHKVSGHAYFSLKDSQSVIRCVLFKGNANRLKFALKEGQEMVVFGGISVYAPRGDYQINCFEIEPKEIGSLTLALEQLKEKLRLKGYFDEANKLPKPNFPKRVAVITSQNSAAWADMKKIASKRWPMCELVCINTLMQGEGCVQSVVESIAYADSFYDTKNAFDAIVVARGGGSMEDLYSFNDEKIADALYLAKTFSMSAIGHESDFLLSDSVADLRASTPSNAMEILLPSSDEWLQRLDGFNVKLHRSFKTLLHQKKAHLEHLAASLKRLSFENKHHLNALKLEKLTIALDNKTLEFLRLKKTLLEKISTQLSTSPFLQTKTERLNRLENALKLAYANLKLPQFGALVSKNHQAIELEALKRGDKIELSNEKARASAEILSVDRV
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_00378}.
Q9ZMI9
FLGI_HELPJ
Flagellar P-ring protein (Basal body P-ring protein)
MKRVFLWLIFVLAFHKLLAEKIGDIASVVGVRDNQLIGYGLVIGLNGTGNKSGSKFTMQSISNMLESVNVKISADDIKSKNVAAVMITASLPPFARQGDKIDIHISSIGDAKSIQGGTLVMTPLNAVDGNIYALAQGAIISGNSSNLLSANIINGATIEREVSYDLFHKNAMTLSLKNPNFKNAIQVQNTLNKVFGNKVAIALDPKTIQITRPERLSMVEFLALVQEIPINYSAKNKIIVDEKSGTIVSGVDIIVHPIVVTSQDITLKITKEPLNDSKNMQDLDNNMSLDTAHNTLSSNGKNITIAGVVKALQKIGVSAKGMVSILQALKKSGAISAEMEIL
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Q9ZMJ6
SYP_HELPJ
Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)
MLFSKLFAPTLKEPPKDAVLKSPKHPGKAGYIYQIGSGIYNFLPLAKKVLDKIENVTHKRMQEHGAQNILMSFVVLASLWEKSGRLDKYGKELLVFKDRKDNDFVLSPTLEENITEIAANFIKSYKQLPVHLYQIHTKFRDEIRPRFGLVRAREFIMKDGYSFHEDAESLDKEFLNTQSAYKEILSDLGLDFRIVEADSGAIGGSKSREFVVLTECGEDTIVVCQNCDYAANIEIAKRSKRTEPLMSPSALAKFPTPNTTSAPSVAEFFKTEPYFVLKALVNKVIHKDKETLACFFVRGDDNLEETKALNTLNLLGANALELREANEEDLNKAGLIAGFIGPYGLKKHVCYIIFDEDLKEGDCLIVGANEKDFHAVGVDLKGFENLVYADIVQVKESDCCPNCQGALKYHKSLEVGHIFKLGQSYAKSLKASFLDKNGKERFFEMGCYGIGISRLLSVILEQKSDDLGCVWTKNTAPFDVVIVVSNLKDEAQKKLAFEVYERLLQKGVDALLDDRDARFGAKMRDFELIGERLALIVGKQTLESKEFECIKRANLEKQTIKDIELEEKILEMLASE
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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. {ECO:0000255|HAMAP-Rule:MF_01569}.
Q9ZMJ9
HCPE_HELPJ
Putative beta-lactamase HcpE (EC 3.5.2.6) (Cysteine-rich protein E)
MNIKILKILVGGLFFLSLNAHLWGKQDNSFLGIGERAYKSGNYSKAASYFKKACNDGVSEGCTQLGIIYENGQGTRIDYKKALEYYKTACQADDREGCFGLGGLYDEGLGTAQNYQEAIDAYAKACVLKHPESCYNLGIIYDRKIKGNAAQAVTYYQKSCNFDMAKGCYILGTAYEKGFLEVKQSNHKAVIYYLKACRLNEGQACRALGSLFENGDAGLDEDFEVAFDYLQKACALNNSGGCASLGSMYMLGRYVKKDPQKAFNYFKQACDMGSAVSCSRMGFMYSQGDTVSKDLRKALDNYERGCDMGDEVGCFALAGMYYNMKDKENAIMIYDKGCKLGMKQACENLTKLRGY
May hydrolyze 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives.
Q9ZMK4
KDSB_HELPJ
3-deoxy-manno-octulosonate cytidylyltransferase (EC 2.7.7.38) (CMP-2-keto-3-deoxyoctulosonic acid synthase) (CKS) (CMP-KDO synthase)
MIIIPARLKSSRFENKMLEDIFGLPMVVRCAKNANLVDECVVACDDESIMKACQKFHIKAVLTSKHHNSGTERCLEAAQILGLKNDERVLNLQGDEPFLEKKVILALLEATQNAPFMATCAKVIDEEQAKSPNLVKVVLDSQNNALYFSRSLIPFLRDFDAKRQTPLLGHIGIYGFHNKEILEELCALKPCVLEDTEKLEQLRALYYQKKILVKIVQSESMGIDTKEDLQNALKIFSPNLLKR
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.
Q9ZML9
MNMG_HELPJ
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG (Glucose-inhibited division protein A)
MVKESDILVVGGGHAGIEASLIAAKMGVRVHLITMLIDTIGLASCNPAIGGLGKGHLTKEVDVLGGAMGIITDHSGLQYRVLNASKGPAVRGTRAQIDMDTYRIFARNLVLNTPNLSVSQEMTESLILENDEVVGVTTNINNTYRAKKVIITTGTFLKGVVHIGEHQNQNGRFGENASNSLALNLRELGFKVERLKTGTCPRVAGNSIDFEGLEEHFGDANPPYFSYKTKDFNPTQLSCFITYTNPITHQIIRDNFHRAPLFSGQIEGIGPRYCPSIEDKINRFSEKERHQLFLEPQTIHKSEYYINGLSTSLPLDVQEKVIHSIKGLENALITRYGYAIEYDFIQPTELTHALETKKIKGLYLAGQINGTTGYEEAAAQGLMAGINAVLALKNQAPFILKRNEAYIGVLIDDLVTKGTNEPYRMFTSRAEYRLLLREDNTLFRLGEHAYRLGLMEQDFYKELEKDKQAIQENLKRLKECVLTPSKEVLKRLNELGENPINDKMDGVSLLARDSFNLEKMRSFFSFLVPLNERVLEQIKIECKYNIYIEKQHENIAKMDSMLKVSIPKHFVFKGIPGLSLEAVEKLEKFRPKSLFEASEISGITPANLDVLHLYIHLRKNS
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}.
Q9ZMM2
HTPG_HELPJ
Chaperone protein HtpG (Heat shock protein HtpG) (High temperature protein G)
MSNQEYTFQTEINQLLDLMIHSLYSNKEIFLRELISNASDALDKLNYLMLTDEKLKGLNTTPSIHLSFDSQKKTLTIKDNGIGMDKSDLIEHLGTIAKSGTKSFLSALSGDKKKDSALIGQFGVGFYSAFMVASKIVVQTKKVTSHQAYAWVSDGKGKFEISECVKEEQGTEITLFLKEEDSHFASRWEIDSVVKKYSEHIPFPIFLTYTDTKFEGEGDNKKEVKEEKCDQINQASALWKMNKSELKEKDYKDFYQSFAHDNSEPLSYIHNKVEGSLEYTTLFYIPSKAPFDLFRVDYKSGVKLYVKRVFITDDDKELLPSYLRFVKGVIDSEDLPLNVSREILQQNKILANIRSASVKKILSEIERLSKDNKNYHKFYEPFGKVLKEGLYGDFENKEKLLELLRFYSKDKGEWISLKEYKENLKENQKSIYYLLGENLDLLKASPLLEKYAQKGYDVLLLSDEIDAFVMPGVNEYDKTPFRDASHSESLKELGLAEIHDEVKDQFKDLIKAFEENLKDEIKGVELSGHLTSAVALIGDEPNAMMANWMRQMGQSVPESKKTLELNPNHAILQKLLKCEDKEQLSAFIWLLYDGAKLLEKGALKDAKSFNERLNSVLLKAL
Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-Rule:MF_00505}.
Q9ZMM5
APBC_HELPJ
Iron-sulfur cluster carrier protein
MLTQEDVLNALKTIIYPNFEKDIVSFGFVKNITLHDNQLGLLIEIPSSSEETSAILRENISKAMQEKGVKALNLDIKTPPKPQAPKPTTKNLAKNIKHVVMISSGKGGVGKSTTSVNLSIALANLNQKVGLLDADVYGPNIPRMMGLQNADVIMDPSGKKLIPLKAFGVSVMSMGLLYDEGQSLIWRGPMLMRAIEQMLSDIIWGDLDVLVVDMPPGTGDAQLTLAQAVPLSAGITVTTPQIVSLDDAKRSLDMFKKLHIPIAGIVENMGSFVCEHCKKESEIFGSNSMSGLLEAYNTQILAKLPLEPKVRLGGDKGEPIVISHPTSVSAKIFEKMAKDLSAFLDKVEREKLADNKDIQPTQTHAYSH
Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040}.
Q9ZMN6
LPXD_HELPJ
UDP-3-O-acylglucosamine N-acyltransferase (EC 2.3.1.191)
MKLSELLSAYSIETEFSNDFEVHALAELDKATPNDISYIDQVCYLKLLKDSKAGAVFIRKKESSKVPKSMQALIVDNPHLAFAKVSHAFKIPFFKNPQSVNEPKHFEKVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVILYQNTILEDNVIIHAGSVIGGDGFGYAHTALGEHVKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIGHNCVLGEHSIVVSQVGLSGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFAGAIPAMEIHEWHHFLAHLRTNFRKQQKTSLLQKAKGFFKS
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00523}.
Q9ZMN9
FRDC_HELPJ
Fumarate reductase cytochrome b subunit (Quinol-fumarate reductase cytochrome b subunit) (QFR cytochrome b subunit)
MQQEEIIEGYYGASKGLKKSGIYAKLDFLQSATGLILALFMIAHMFLVSSILISDEAMYKVAKFFEGSLFLKAGEPAIVSVVAAGVILILVAHAFLALRKFPINYRQYKVFKTHKHLMKHGDTSLWFIQALTGFAMFFLASIHLFVMLTEPESIGPHGSSYRFVTQNFWLLYIFLLFAVELHGSIGLYRLAIKWGWFKNVSIQGLRKIKWAMSVFFIVLGLCTYGAYIKKGLENKDNGIKTMQEAIEADGKFHKE
The fumarate reductase enzyme complex is required for fumarate respiration. This subunit anchors the complex in the membrane and binds a diheme cytochrome b.
Q9ZMQ5
EFP_HELPJ
Elongation factor P (EF-P)
MAIGMSELKKGLKIELGGVPYRIVEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLVEKTMQYLYHDGDTYQFMDIESYEQIALNDSQVGEASKWMLDGMQVQVLLHNDKAISVDVPQVVALKIVETAPNFKGDTSSASKKPATLETGAVVQVPFHVLEGETIKVNTETEEYLEKVK
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).
Q9ZMR1
RF2_HELPJ
Peptide chain release factor 2 (RF-2)
MDNYTYSELLKSLQNKCDNIALIIKPEKIKQELERIEKEQEDPNFWQDVLKARDTNKEKVRLNRLLETYQKMKNSLDESVELFELAQNDSDEVTLSLLYEEAPTLEHSVQKVEIEIMLSGENDASNAIITIQPGAGGTESQDWASILYRMYLRWAERKSFKSEILDYQDGEEAGIKGVAFIIKGENAYGYLKNENGVHRLVRISPFDANAKRHTSFASVQISPELDDDIDIEIDEKDVRYDYYRASGAGGQHVNKTESAVRITHFPTGIVVQCQNDRSQHKNKASALKMLKSKLYELELEKQQSSAKNEEKSEIGWGHQIRSYVLAPYQQVKDARSNIAYSNVEAILDGDIDAILEGVLIAKA
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
Q9ZMR3
TRHP_HELPJ
tRNA hydroxylation protein P (EC 3.4.-.-)
MNQVELLSPAGNLKKLKIALNYGADAVYGGVSHFSLRNRAGKEFTLETFKEGIDYAHALDKKVYATINGFPFNSQLKLLEEHLYKMAELEPDAFIIAAPGVIKLASKIAPHIPVHLSTQANVLNTLDAQVFYDLGVKRIVCARELSLNDAVEIKKALPDLELEIFVHGSMCFAFSGRCLISALQKGRVPNRGSCANDCRFDYEYYVKNPDNGVMMRLVEEEGVGTHIFNAKDLNLSGHIAEILSSNAISALKIEGRTKSSYYAAQTTRIYRLAVDDFYHNTLKPSFYASELNTLKNRGFTDGYLMRRPFERLDTQNHQTAISEGDFQVNGEITEDGRFFACKFTTTTNTAYEIIAPKNAAITPIVNDIGKIYTFEKRSYLVLYKILLENNTELETIHSGNVNLVRLPAPLPAFSFLRTQVRV
Involved in prephenate-dependent formation of 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5-carboxymethoxyuridine (cmo5U) biosynthesis.
Q9ZMS7
RECA_HELPJ
Protein RecA (Recombinase A)
MAIDEDKQKAISLAIKQIDKVFGKGALVRLGDKQVEKIDAISTGSLGLDLALGIGGVPKGRIIEIYGPESSGKTTLSLHIIAECQKNGGVCAFIDAEHALDVYYAKRLGVDTENLLVSQPSTGEEALEILETITRSGGIDLVVVDSVAALTPKAEIDGDMGDQHVGLQARLMSHALRKITGVLHKMNTTLIFINQIRMKIGMTGYGSPETTTGGNALKFYASVRIDIRRIAALKQNEQHIGNRAKAKVVKNKVAPPFREAEFDIMFGEGISKEGEIIDYGVKLDIVDKSGAWLSYQDKKLGQGRENAKALLKEDKALADEITLKIKESIGSNEEIMPLPDEPLEEME
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. {ECO:0000255|HAMAP-Rule:MF_00268}.
Q9ZMV1
RL20_HELPJ
Large ribosomal subunit protein bL20 (50S ribosomal protein L20)
MRVKTGVVRRRRHKKVLKLARGFYSGRRKHFRKAKEQLERSMYYAFRDRKQKKREFRSLWVVRINAACRMHNTSYSRFMHALKVANIELDRKVLADMAMNDMQAFKSVLESVKEHL
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).
Q9ZMV2
IF3_HELPJ
Translation initiation factor IF-3
MSRNEVLLNGDINFKEVRCVGDNGEVYGIISSKEALKIAQNLGLDLVLISASAKPPVCKVMDYNKFRYQNEKKIKEAKKKQKQIEIKEIKLSTQIAQNDINYKVKHAREFIESNKHVKFKVVLKGRESQNSKAGLDVLFRVQTMMQDLANPEKEPKTEGRFVSWMFVPKAKEAPKNEKKTKENNPPFNRINLMKGENHAKNED
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}.
Q9ZMW3
GRPE_HELPJ
Protein GrpE (HSP-70 cofactor)
MKDEHNQEHDHLSPKEPESYQKAYACKEQQGEEKQEASEKEGEIKEDFELKYQEMREQYLRVHADFENVKKRLERDKSMALEYAYEKIALDLLPVIDALLGAHKSAVEVDKESALTKGLELTMEKLHEVLARHGIEGIECLEEFDPNFHNAIMQVKSEEKENGKIVQVLQQGYKYKGRVLRPAMVSIAKND
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}.
Q9ZMX5
THRC_HELPJ
Threonine synthase (TS) (EC 4.2.3.1)
MPFVPTRSLKERKIDFIEAVLNPNAPKGGLYTLEHFETLEWQDCLGMSYSELVEHVFELLNLEIPKNLLASALKRYENFDNPKNPAPIFALNERLFVQELYHGPSLAFKDMALQPLASLFSNLAVGKNEKYLVLVSTSGDTGPATLEGLAGMPNVFVVCLYPKDGTSLVQKLQMVTQNASNLKVFGVSGDFDDAQNALKNLLKDDDFNEALKARQLKLSVANSVNFGRIAFQIVYHIWGFLELYKKGAINSKEKITLAIPSGNFGNALGAFYAKKMGLNIAKIKVVTNSNDVLREFIETGRYDLTKRSLKQTFSPAMDILKSSNVERALFSLFGFERTLELMQALEEEKFYALKPKELALLQEHFSCASCSDEDCLKTIQEVYAEHQYLIDPHTATALNASLKTHEKTLVSATASYEKFPKTTLLALNEQKKNDDDKAALETLKNSYNTPDSQRLDDLFERGIKHQEVLKLNEIKSSILLWLENTH
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Q9ZMY3
RPOD_HELPJ
RNA polymerase sigma factor RpoD (Sigma-70)
MKKKANEEKAPKRAKQEAKTEATQENKAKESNKENKNNKAKEGKIKEAKTKESKVKETAKEPIPVKKLSFNEALEELFANSLSDCVSYESIIQISAKVPTLAQIKKIKELCQKYQKKLVSSSEYAKKLNAIDKIKNTEEKQKVLDEELEDGYDFLKEKDFLEWSRSDSPVRMYLREMGDIKLLSKDEEIELSKQIRLGEDIILDAICSVPYLIDFIYAYKDALINRERRVKELFRSFDDDDENSVSDPKKDDDSEEDEENEERKKVVSEKDKKRVEKVQESFKALDKAKKEWLKALEAPIDEKEDELVRSLTLAYKRQTLKDRLYDLEPTSKLINELVKTMETTLKSGDGFEKELKRLEYKLPLFNDTLIANHKKILANITNMTKEDIIAQVPEATMVSVYMDLKKLFLTKEASEEGFDLAPNKLKEILEQIKRGKLISDRAKNKMAKSNLRLVVSIAKRFTSRGLPFLDLIQEGNIGLMKAVDKFEHEKGFKFSTYATWWIKQAISRAIADQARTIRIPIHMIDTINRINKVMRKHIQETGKEPDLEVVAEEVGLSLDKVKNVIKVTKEPISLETPVGNDDDGKFGDFVEDKNIVSSIDHIMREDLKAQIESVLDQLNEREKAVIRMRFGLLDDESDRTLEEIGKELNVTRERVRQIESSAIKKLRSPQYGRILRNYLRI
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. {ECO:0000255|HAMAP-Rule:MF_00963}.
Q9ZMY5
MQO_HELPJ
Malate:quinone oxidoreductase (EC 1.1.5.4) (MQO) (Malate dehydrogenase [quinone])
MSMEFDAVIIGGGVSGCATFYTLSEYSSLKRVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTPEKAKKVRLSAYKTRQYALNKGLQNEVIFETQKMAIGVGDEECEFMKKRYESFKEIFVGLEEFDKQKIKELEPNVILGANGIDRHENIIGHGYRKDWSTMNFAKLSENFVEEALKLKPNNQVFLNFKVKKIEKRNDTYAVISEDAEEVYAKFVLVNAGSYALPLAQSMGYGLDLGCLPVAGSFYFVPDLLRGKVYTVQNPKLPFAAVHGDPDAVIKGKTRIGPTALTMPKLERNKCWLKGISLELLKMDLNRDVFKIAFDLMSDKEIRNYVFKNMVFELPIIGKRKFLKDAQKIIPTLSLEDLEYAHGFGEVRPQVLDRTKRKLELGEKKICTHKGITFNMTPSPGATSCLQNALVDSQEIAAYLGESFELERFYKDLSPEELEN
Catalyzes oxidation of malate to oxaloacetate in the citric acid cycle. Donates electrons to quinones of the electron transfer chain (By similarity).
Q9ZMY6
RL13_HELPJ
Large ribosomal subunit protein uL13 (50S ribosomal protein L13)
MTKTAKVNDIVRDWVVLDAKDKVFGRLITEIAVLLRGKHRPFYTPNVDCGDFVVVINANKVKFSGMKLEDKEYFTHSGYFGSTKSKTLQEMLEKTPEKLYHLAVRGMLPKTKLGKAMIKKLKVYRDDKHPHTAQTSKKDAK
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}.
Q9ZMZ0
RF1_HELPJ
Peptide chain release factor 1 (RF-1)
MSILAEKLSSILKRYDELTALLSSVEVVSDIKKLTELSKEQSSIEEISVASKEYLSVLEGIKENKELLEDKELSELAKEELKILEIQKSELETAIKQLLIPKDPNDDKNIYLELRAGTGGDEAGIFVGDLFKAYCRYADLKKWKVEIVSSSENSVGGYKEIIVLIKGKGVYSRLKFEAGTHRVQRVPETESQGRIHTSAITVAIMPEVDDVEVSINPSDLKIEVFRAGGHGGQCVNTTDSAVRITHLPTNISVSMQDEKSQHKNKDKALKILKARLYEKQIEEQQLANAKDRKEQVGSGDRSERIRTYNYPQNRLSEHRINLTLYSLEEIMLSGNLDEVINPLIAHAQSQFE
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Q9ZMZ1
RS20_HELPJ
Small ribosomal subunit protein bS20 (30S ribosomal protein S20)
MANHKSAEKRIRQTIKRTERNRFYKTKVKNIIKAVREAVAINDVAKAQERLKIANKELHKFVSKGILKKNTASRKVSRLNASVKKIALA
Binds directly to 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_00500}.
Q9ZMZ5
UREE_HELPJ
Urease accessory protein UreE
MIIERLVGNLRDLNPLDFNVDHVDLEWFETRKKIARFKTRQGKDIAIRLKDAPKLGLSQGDILFKEEKEIIAVNILDSEVIHIQAKSVAEVAKICYEIGNRHAALYYGESQFEFKTPFEKPTLALLEKLGVQNRVLSSKLDSKERLTVSMPHSEPNFKVSLASDFKVVVK
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. {ECO:0000255|HAMAP-Rule:MF_00822}.
Q9ZMZ6
UREF_HELPJ
Urease accessory protein UreF
MDKGKSVKSTKKSVGMPPKTPKTDNNANSHVDNEFLILQVNDAVFPIGSYTHSFGLETYIQQKKVTNKESALEYLKANLSSQFLYTEMLSLKLTYESTLQQDLKKILGIEEVIMLSTSPMELRLANQKLGNRFIKTLQAMNELDMGAFFNAYAQTTKDPTHATSYGVFAASLNMELKKALRHYLYAQTSNMVINCVKSVPLSQNDGQKILLSLQSPFNQLIEKTLELDESHLCAASVQNDIKAMQHESLYSRLYMS
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. {ECO:0000255|HAMAP-Rule:MF_01385}.
Q9ZMZ7
UREG_HELPJ
Urease accessory protein UreG
MVKIGVCGPVGSGKTALIEALTRHMSKDYDMAVITNDIYTKEDAEFMCKNSVMPRDRIIGVETGGCPHTAIREDASMNLEAVEEMHGRFPNLELLLIESGGDNLSATFNPELADFTIFVIDVAEGDKIPRKGGPGITRSDLLVINKIDLAPYVGADLKVMERDSKKMRGEKPFIFTNIRAKEGLDDVIAWIKRNALLED
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. {ECO:0000255|HAMAP-Rule:MF_01389}.
Q9ZMZ8
UREH_HELPJ
Urease accessory protein UreH
MNTYAQESKLRLKTKIGADGRCVIEDNFFTPPFKLMAPFYPKDDLAEIMLLAVSPGLMKGDAQDMQLNIGPNCKLRITSQSFEKIHNTEDGFASRDMHIVVGENAFLDFAPFPLIPFENAHFKGNTTISLRSSSQLLYSEIIVAGRVARNELFKFNRLHTKISILQDEKPIYYDNTILDPKTTNMNNMCMFDGYTHYLNLVLVNCPIELSGARELIEESEGVDGAVSKIASSHLCLKALAKGSEPLLHLREKIARLVTQTTTQKV
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. {ECO:0000255|HAMAP-Rule:MF_01384}.
Q9ZN29
Y031_HELPJ
Nucleoid-associated protein jhp_0031
MDFSQLGGLSGLLDGVKKEFSQLEEKNKDTIHTSKSGGGMVSVSFNGLGELVDLQIDDSLLEDKEAMQIYLMSALNDGYKAVEENRKNLAFNMLGNFAKL
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. {ECO:0000255|HAMAP-Rule:MF_00274}.
Q9ZN32
CLPS_HELPJ
ATP-dependent Clp protease adapter protein ClpS
MKMHQIPTPTMSQVIMLNDSITTAEFMVSALRDFFDKPLEEAQKLMLSIHRDGDGVCGVYPYEIAIYKAVCVRDKARARFPLRLMVQEVK
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. {ECO:0000255|HAMAP-Rule:MF_00302}.
Q9ZN56
RISB_HELPJ
6,7-dimethyl-8-ribityllumazine synthase (DMRL synthase) (LS) (Lumazine synthase) (EC 2.5.1.78)
MQIIEGKLQLQGNEKIAILTSRFNHIITDRLKEGAMDCFKRHGGDEELLDLVLVPGAYELPLILDKLLESGKYDGVCVLGAIIRGGTPHFDYVSAEATKGIASAMLKYSMPVSFGVLTTDNIEQAIERAGSKAGNKGFEAMSTLIELLSLCQTLKD
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}.
Q9ZN57
NUSB_HELPJ
Transcription antitermination protein NusB (Antitermination factor NusB)
MATRTQARGAVVELLYAFESGNEEIKKIASSMLEEKKIKNNQLAFALSLFNGVLEKINEIDALIEPHLKDWDFKRLGSMEKAILRLGAYEIGFTPTQNPIIINECIELGKLYAEPNTPKFLNAILDSLSKKLAQKPLI
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}.
Q9ZN79
LINR_SPHIU
HTH-type transcriptional regulator LinR
MNIDDLDFRHLVLLDALLKRHSVSAAARELDLPQPTASHGLARLRKALGDPLLVRARDGMEPTPRAEAIAGVVQQLLELRRDLAEGGQTFSPDRLKREFIIAGSDIAHLVVLTALHSAARFEAPHTSYRALTLSGDEMVSALETGHVDIAVGAYPSLVAGIKTQRLYQEEYLCFGKEGHPFIKSGETDDFMAADHIVVSTKGMAHAHRAVERALLDKIHPDRIRIVASSFLVALAACFESDLILTAPARVIGRLAEVYGLRAVRPPILMEAFEVRQYWHARNQDDPPHRWLRQLLHKVLSARM
Positively regulates the transcription of the linD and linE genes that are involved in gamma-hexachlorocyclohexane (gamma-HCH or lindane) degradation. This degradation pathway allows S.japonicum UT26 to grow on gamma-HCH as the sole source of carbon and energy.
Q9ZNA2
RECR_DEIRA
Recombination protein RecR
MKYPPSLVSLIRELSRLPGIGPKSAQRLAFHLFEQPREDIERLASALLEAKRDLHVCPICFNITDAEKCDVCADPSRDQRTICVVEEPGDVIALERSGEYRGLYHVLHGVLSPMNGVGPDKLHIKPLLPRVGQGMEVILATGTTVEGDATALYLQRLLEPLGAAISRIAYGVPVGGSLEYTDEVTLGRALTGRQTVSKPQPPQRPGDEDGADGAAVPASR
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}.
Q9ZNA5
SAHH_ROSDO
Adenosylhomocysteinase (EC 3.13.2.1) (S-adenosyl-L-homocysteine hydrolase) (AdoHcyase)
MTKDFIVKDIALAEFGRKELDIAETEMPGLMALRAEYGDSKPLAGARIVGSLHMTIQTAVLIETLVALGADVRWASCNIFSTQDHAAAAIAAGGTPVFAIKGQSLEEHWDYLDRSFMFEDGPNLILDDGGDATLYVLLGARAEAGEEIIPVPTSEEEEAIKAQIKKRMAASPGWFTKVRDQIKGVSEETTTGVHRLYDLVKQGQLPFPAINVNDSVTKSKFDNKYGCKESLVDGIRRATDTMMAGKVAVVMGYGDVGKGSAASLRGAGARVKVTEVDPICALQAAMDGFEVVLLEDVVGSADIFITTTGNKDVIRIEHMRAMKDMAIVGNIGHFDNEIQVAALKNHKWTNIKEQVDMIEMPNGNRLILLSEGRLLNLGNATGHPSFVMSASFTNQVLAQIELWTRADAYDNEVYILPKHLDEKVARLHLDRIGVKLTPLDPEQAAYIGVKPEGPFKPEHYRY
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-Rule:MF_00563}.
Q9ZNB7
ALGL_COBMA
Alginate lyase (EC 4.2.2.3) (Poly(beta-D-mannuronate) lyase)
MRNPKLKNLLAPTLLSLAMFAGATQAAAPLRPPQGYFAPVDKFKTGDKSDGCDAMPAPYTGPLQFRSKYEGSDKARATLNVQSEKAFRDTTKDITTLERGTAKRVMQFMRDGRPEQLECTLNWLTAWAKADALMSKDFNHTGKSMRKWALGSMASSYIRLKFSDSHPLAQHQQEAQLIEAWFSKMADQVVSDWDNLPLEKTNNHSYWAAWSVMATAVATNRRDLFDWAVKEYKVGVNQVDADGFLPNELKRQQRALAYHNYALPPLAMIASFAQINGVDLRQENNGALKRLGDRVLAGVKDPDEFEEKNGKKQDMTDLKEDMKFAWLEPFCTLYTCAPDVIEKKRDMQPFKTFRLGGDLTKVYDPSHEKGNKGS
Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism. May serve to degrade mislocalized alginate that is trapped in the periplasmic space. {ECO:0000255|HAMAP-Rule:MF_00557}.
Q9ZNE7
SECE_VIBAL
Protein translocase subunit SecE
MKANNAETPDSSNAADTFKWLAAFVLAAAAVVGNYLYGEMSVVVRAAGVVVLIAAALGVAATTTKGKAAISFAKESRMEVRKVVWPTRQETMQTTLIVLAVSIVMALVLWGIDGIMVRLVALATGV
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. {ECO:0000255|HAMAP-Rule:MF_00422}.
Q9ZNJ6
RUVA_HATHI
Holliday junction branch migration complex subunit RuvA
MYEYIKGTYMGINKEYIVIENGDIGYKIHSSGYTIANMPNIGEHIMLYLTQIVREDFIGLYGFGSKEELELFNKLLTVNGIGAKASLSLLSITNVENLKRAIVLEDEKLLIKAPGIGKKTAQRIILELKDKLDVNLDEGIQTDSNDIKVSSKILEEAKEALMSLGYSEKECEKALKNVEEKESLEIIIKESLKFLMN
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}.
Q9ZNS0
PLT3_ARATH
Probable polyol transporter 3
MVHADGHNFPGSDPNPHMNKFAFGCAIVASIISIIFGYDTGVMSGAQIFIRDDLKINDTQIEVLAGILNLCALVGSLTAGKTSDVIGRRYTIALSAVIFLVGSVLMGYGPNYPVLMVGRCIAGVGVGFALMIAPVYSAEISSASHRGFLTSLPELCISLGILLGYVSNYCFGKLTLKLGWRLMLGIAAFPSLILAFGITRMPESPRWLVMQGRLEEAKKIMVLVSNTEEEAEERFRDILTAAEVDVTEIKEVGGGVKKKNHGKSVWRELVIKPRPAVRLILIAAVGIHFFEHATGIEAVVLYSPRIFKKAGVVSKDKLLLATVGVGLTKAFFIIIATFLLDKVGRRKLLLTSTGGMVFALTSLAVSLTMVQRFGRLAWALSLSIVSTYAFVAFFSIGLGPITWVYSSEIFPLRLRAQGASIGVAVNRIMNATVSMSFLSMTKAITTGGVFFVFAGIAVAAWWFFFFMLPETKGLPLEEMEKLFGGGGPRGDRDGLEIQTKTISIGGFS
Plasma membrane sugar-proton symporter.
Q9ZNU9
SAP3_ARATH
Zinc finger A20 and AN1 domain-containing stress-associated protein 3 (AtSAP3)
MAEEHRLQEPRLCANNCGFFGSTATQNLCSKCFRDLQHQEQNSSTAKHALTQSLAAVGAAASSSVSPPPPPPADSKEIVEAKSEKRAAAEPEEADGPPQDPKRCLTCRRRVGITGFRCRCGFVFCGTHRYAEQHECSFDFKRMGKDKIAKANPIVKADKLEKI
May be involved in environmental stress response.
Q9ZP21
TRXM_WHEAT
Thioredoxin M-type, chloroplastic (Trx-M)
MALETCLRGWALYAPQAGIRERLSSGSYAPSRPRTAAPAVVSPSPYKSALVAARRPSRFVCKCKNVVDEVIVADEKNWDNMVIACESPVLVEFWAPWCGPCRMIAPVIDELAKDYVGKIKCCKVNTDDCPNIASTYGIRSIPTVLMFKDGEKKESVIGAVPKTTLCTIIDKYIGS
Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase (By similarity).
Q9ZP40
PG1_PEA
Plastoglobulin-1, chloroplastic
MALLSSTLRAPLVFSKNPKPVSLSSLHSRIYLSPRSPRFPSLRFISAAGDTGDAEKPSSNISDEWGEGSEPETKPFTYFKLPDSDPPKDEDEWGKGAAAGAGSYNDAGNGTPTFAAEASPEAEAEDGVDENLEGLKRSLVDTVYGTELGFRARSEVRAEVSEFVAQLEAANPTPAPVEEPDLLNGNWVLLYTASSELLPLLAAGSLPLLKLDKISQTIDTDSFTVVNSTTLSSPFASFSFSVSASFEVRSPTRIQVTFKEGSLQPPEIKSKIDLPENINIFGQQLSLGPLLQSLGPLENVVANISRVISGQSPLKIPIPGERTSSWLITTYLDKDLRISRGDGGLFVLAREGSSLLDQ
May form together with other plastoglobulins a coat on the surface of the lipoprotein particle. The coat may contain receptors for attachment to the thylakoid membrane as well as regulatory proteins that may function in the transfer of lipids to and from the thylakoid membranes.
Q9ZP55
DRP4C_ARATH
Dynamin-related protein 4C
MVKKKVATKKNSPSLAIAKKKSRSNKDVVSVEAPIISSYNDRIRPLLDTVDRLRNLNVMREGIHLPTIVVVGDQSSGKSSVLESLAGISLPRGQGICTRVPLVMRLQRSSSPEPEIWLEYNDKVVPTDEEHIAEAIRAATDVIAGSGKGVSDAPLTLHVKKAGVPDLTMVDLPGITRVPVNGQPENIYEQISGMIMEYIEPQESIILNVLSATVDFTTCESIRMSRKVDKTGQRTLAVVTKADMAPEGLLQKVTADDVSIVLGYVCVRNRIGEETYEEARMQEELLFRTHPVLSLIDEDIVGIPVLAQKLMLIQSSMIARCLPKIVSKINQKLDTAVLELNKLPMVMASTGEALMALMDIIGSAKESLLRILVQGDFSEYPDDQNMHCTARLADMLSQFSDSLQAKPKEVAEFLMDEIKILDECKCVGLPNFIPRSAFLAILSQHVDGIQDKPVEFINKIWDYIEDVLSSVTAKRSDNFPQIQSSIKRAGRNLISKIKEQSVNRVMEIVEMEKLTDYTCNPEYMTSWTQKTSAQESFIDAVVKNENIPDYFSVTGFGNVKISHLRKYHAHLLIPAFDMKMRITSYWKIVLRRIVDNLALYLQLSVKSLVNTRFQKEIVAEMVDPRDGGGVEKMLEESPLVASKREKLQNSIKLLKESKDAVAAIVDQNC
Putative microtubule-associated force-producing protein, able to bind and hydrolyze GTP.
Q9ZPQ8
ACR5_ARATH
ACT domain-containing protein ACR5 (Protein ACT DOMAIN REPEATS 5)
MDVCLSYSYNMDDEIAKFIRRVNPPRVVIDNEVCKDVTVIKVDSANKHGILLEVVQVLTELNLTIKKAYISSDGGWFMDVFNVTDQDGNKVTDEIVLEYIRKSLGPDESSCFSPSMRSTIGVKQSVDYTVVELTGTDRPGLLSELCAVLMDLQCNVVNAEIWTHRAKAAAVLQVTDEETCSAITDPERLSKIRKLLGYVLTGGSSGRRFREPKTTVSSALNETHTDRKLHQLMFADRDYDEWENNVDDEDKCGRVIPDVDVSNLHDLDYSIVMIKCKDRPKLLFDTVFTLTDMNYVVSHASIDAEGPQAYQEYYIRHTDGSPVKSEAERQRVIKCLKAAIQRRVSEGLKLELCTSDRVGLLSDVTRIFRENSLTVTRAEVKTKGDKALNTFYVRDASGYQVDTKTIESIRQVIGQTILQVKGGNTDAKPSPQDSPTGFLFGVFKSRSFVNFGLIRS
May bind amino acids.
Q9ZPR0
COQ4_ARATH
Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial (Coenzyme Q biosynthesis protein 4 homolog)
MIIERARVPLSRWQQAAVAMGSALGALVDPRRADLIAALGETTGKPAFEMVLERMKKSEEGRAILLERPRVVSEQVGHAWDLPENTFGAAYAKFMGSRNFSPDDRPPVRFMETDELAYVATRAREVHDLWHTLFGLPTNLIGESSLKVIEFEQMYLPMCMLSVIGGTVRFNEKQRSMFLKHYLPWAVRAGRQCTDLMCVYYERHFSEDLEQVRRKWGIIPAPQHPK
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides. {ECO:0000255|HAMAP-Rule:MF_03111}.
Q9ZPR1
CD48B_ARATH
Cell division control protein 48 homolog B (AtCDC48b)
MLETESSVCDNIAGNEKWRAEAEIGGNERALQALRELIIFPFRYPLEARTLGLKWPRGLLLYGPPGTGKTSLVRAVVQECDAHLIVLSPHSVHRAHAGESEKVLREAFAEASSHAVSDKPSVIFIDEIDVLCPRRDARREQDVRIASQLFTLMDSNKPSSSAPRVVVVASTNRVDAIDPALRRAGRFDALVEVSTPNEEDRLKILQLYTKKVNLDPSVDLQAIAISCNGYVGADLEALCREATISASKRSSDSLILTSQDFKIAKSVVGPSINRGITVEIPKVTWDDVGGLKDLKKKLQQAVEWPIKHSAAFVKMGISPMRGILLHGPPGCSKTTLAKAAANAAQASFFSLSCAELFSMYVGEGEALLRNTFQRARLASPSIIFFDEADVVACKRGDESSSNSSTVGERLLSTLLTEMDGLEEAKGILVLAATNRPYAIDAALMRPGRFDLVLYVPPPDLEARFEILQVHTRNMTLGDDVDLRKIAEETDLFTGAELEGLCRESGTVSLRENIAATAVFNRHFQTAKSSLKPALTIEEVETYSSFRKAAKRSDSKPIPINKKKATSTVFGFSWQLGVLSLLLLATGNYYFNHTKHELLVASAT
Probably functions in cell division and growth processes. Interacts with certain SNAREs as part of specialized membrane fusion events where vesicles from the same organelle fuse (homotypic fusion) (By similarity).
Q9ZPR4
MRS25_ARATH
Magnesium transporter MRS2-5 (Magnesium Transporter 3) (AtMGT3)
MGEQLDPFSASNLPDFISSQKIGRPVNFEGQTNRGHPFSGLKKRGQSSRSWVKIDQDGNSAVLELDKATIMKRCSLPSRDLRLLDPLFIYPSSILGRERAIVVSLEKIRCIITAEEVILMNARDASVVQYQSELCKRLQSNHNLNVKDDLPFEFKALELVLELSCLSLDAQVNELEMEVYPVLDELATNISTLNLEHVRRLKGRLLTLTQKVQKVCDEIEHLMDDDDDMAEMYLTEKKERAEAHASEELEDNIGEDFESSGIVSKSAPVSPVGSTSGNFGKLQRAFSSIVGSHKSLLSSSSIGENIDQLEMLLEAYFVVVDNTLSKLSSLKEYIDDTEDLINIKLGNVQNQLIQFQLLLTAATFVAAIFAAVTAVFGMNLQDSVFQNPTTFQYVLLITGIGCGFLYFGFVLYFKHKKVFPL
Magnesium transporter that may mediate the influx of magnesium.
Q9ZPR6
UPS3_ARATH
Ureide permease 3 (AtUPS3)
MYVIESKGGTITCMLLALLFLGTWPAIMTLTERRGRLPQHTYLDYTLTNLLAAVIIAFTLGEISPSRPNFTTQLSQDNWPSVMFAMAGGIFLSLGTLATQYAWAFVGLSVTEVITASIAVVIGTTLNYFLDDRINRAEVLFPGVACFLIAVCFGSAVHKSNAADNKSKLQGFKSLETTSSFQMETSSIKEGKAKVGTADFLIEVEKQRAIKVFGKSTIIGLAITFFAVPKLNVYTAFFYFSISSFGVGLILNIIFLYWPILGLPRSSFKAYLNDWNGRGWSFLAGFLCGFGNGLQFMGGQAAGYAAAGAVQIENKHFGGYCCLENTKDHQEKHIHFLSVCYLCS
Proton-coupled transporter that transports a wide spectrum of oxo derivatives of heterocyclic nitrogen compounds.