entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
|
|---|---|---|---|---|
Q9Z7K8
|
EFTS_CHLPN
|
Elongation factor Ts (EF-Ts)
|
MSDFSMETLKTLRQQTGVGLTKCKEALEACGGNLEEAVVYLRKLGLASAGKKEHRETKEGIIAAKTDANGTALIEVNVETDFVANNAVFREFVSNLLNDILKYKVDTVEALSQAASSQDPSLSVDELRAVTMQTVGENIRISRVAYFPKATNSTVGIYSHGNGKTVALTMLSGSSTADSLAKDIAMHVVAAQPQFLSKESVPAEAIAKEKEVIASQIQGKPQEVIEKIVTGKLNTFFQEACLLEQPFIKNADLSIQSLIDDFSKTSGSSVAIEQFILWKIGA
|
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).
|
Q9Z7L5
|
CSD_CHLPN
|
Probable cysteine desulfurase (EC 2.8.1.7)
|
MKNLKEDFPIFAAKAKENEPFIYLDSAATTQKPQQVIDAVANFYTSSYATVNRAIYSSSRNVTEAYAAVREKVRKWVSAASDSEIVFTRGTTAGLNLLAISVNDLWIPKGGVVLVSEAEHHANVLSWEIACRRRGSLVKKIRVHDSGLIDLDDLEKLLNEGAQFVSIPHVSNVTGCVQPLQQVAELVHRYDAYLAVDGAQGAPHLPIDVQLWDVDFYVFSSHKIYGPTGIGVLYGKKDLLDQLPPVEGGGDMVAIYDHQNPEYLPAPMKFEAGTPNIAGVLGLGAALDYLDGLSAKFIYDKEIALTTYLHKELLEIPGVEILGPSIEEPRGALIGMTIDGAHPLDLGFLLDLRGIAVRTGHQCAQPAMERWNVGHVLRVSLGIYNDEDDIDQFILVLQDSLDKIRR
|
Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
|
Q9Z7M0
|
PARB_CHLPN
|
Probable chromosome-partitioning protein ParB
|
MTEEISKDTIIEVAIDDIRVSPFQPRRVFSNEELQELIASIKAVGLIHPPVVREICTGDRVLYYELIAGERRWRAMQLAGATTIPVILKHVIADGTAAEATLIENIQRVNLNPIEMAEAFKRLIHVFGLTQDKVAYKVGKKRSTVANYLRLLALSKTIQESLLQGQITLGHAKVILTLEDPILREKLNEIIIQEHLAVREAELIAKQLISEEGSSIELKPTPLDMAESSKQHEELQQRLSDLCGYKVQIKTRGSKATVSFHLQNTQDLQKLEAWLSSHGTLSESLS
|
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).
|
Q9Z7M4
|
Y680_CHLPN
|
Putative phosphate permease CPn_0680/CP_0067/CPj0680/CpB0707
|
MLPLIIFVLLCGFYTSWNIGANDVANAVGPSVGSGVLTLRQAVVIAAIFEFFGALLLGDRVAGTIESSIVSVTNPMIASGDYMYGMTAALLATGVWLQLASFFGWPVSTTHSIVGAVIGFGLVLGKGTIIYWNSVGIILISWILSPFMGGCVAYLIFSFIRRHIFYKNDPVLAMVRVAPFLAALVIMTLGTVMISGGVILKVSSTPWAVSGVLVCGLLSYIITFYYVHTKHCSYISDTPKKGSLTYRLKERGGNYGRKYLVVERIFAYLQIIVACFMAFAHGSNDVANAIAPVAGVLRQAYPASYTSYTLIRLMAFGGIGLVIGLAIWGWRVIETVGCKITELTPSRGFSVGMGSALTIALASILGLPISTTHVVVGAVLGIGLARGIRAINLNIIKDIVLSWFITLPAGALLSILFFFALRALFH
|
Potential transporter for phosphate.
|
Q9Z7N8
|
DPO3A_CHLPN
|
DNA polymerase III subunit alpha (EC 2.7.7.7)
|
MTWIPLHCHSQYSVLDAMSSIKDFVAKGQEFGIPALALTDHGNLYGAVDFYKECTQKGIQPIIGCECYIAPGSRFDKKKEKRSRAAHHLILLCKNEQGYRNLCILTSLAFTEGFYYFPRIDKDLLRQYSEGLICLSGCLSSSVSDAALKSPEALLLELQWFQDLFKDDYFTEVQLHKMSEESIAGFKEEWLKQEYYSLIEKQIKVNTAVLEASKRLGIPTVATNDIHYINANDWQAHEILLNVQSGETVRIAKQNTHIPNPKRKVYRSREYYFKSPAQMAELFKDIPEVISNTLEVAKRCDFTFDFSKKHYPIYVPESLKTLNSYTEEDRYQASAVFLKQLAEEALPKKYSSEVLAHIAKKFPHRDPIDIVKERMDMEMAIIIPKGMCDYLLIVWDIIHWAKANGIPVGPGRGSGAGSVLLFLLGITEIEPIRFDLFFERFINPERLSYPDIDIDICMAGRERVINYAIERHGKDNVAQIITFGTMKAKMAVKDVGRTLDMALSKVNHIAKHIPDLNTTLSKALETDPDLHQLYINDAESAQVIDMALCLEGSIRNTGVHAAGVIICGDQLTNHIPICISKDSTMITTQYSMKPVESVGMLKVDLLGLKTLTSINIAMSAIEKKTGQSLAMATLPLDDATTFSLLHQGKTMGIFQMESKGMQELAKNLRPDLFEEIIAMGALYRPGPMDMIPSFINRKHGKEIIEYDHPLMESILKETYGIMVYQEQVMQIAGALASYSLGEGDVLRRAMGKKDFQQMEQEREKFCKRACNNGIDPELATVIFDKMEKFAAYGFNKSHAAAYGLITYTTAYLKANYPKEWLAALLTCDSDDIEKIGKLIREAQSMGIPILPPHINVSSNHFVATDEGIRFAMGAIKGIGRGLIESIVEERDHHGPYESIRDFIQRSDLKKVSKKSIESLIDAGCFDCFDSNRDLLLASVEPLYEAIAKDKKEAASGVMTFFTLGAMDRKNEVPICLPKDIPTRSKKELLKKEKELLGIYLTEHPMDTVRDHLSRLSVVLAGEFENLPHGSVVRTVFIIDKVTTKISSKAQKKFAVLRVSDGIDSYELPIWPDMYEEQQELLEEDRLIYAILVLDKRSDSLRISCRWMKDLSIVNENIIYECDQAFDRIKNQVQKMSFTMSTSGKETKAKGNKPNENGHTQALAPVTLSLDLNELRHSHLCILKKIVQKHPGSRTLVLVFTQDNERVASMSPDDAYFVCEDIEELRQELVTADLPVRVITV
|
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity).
|
Q9Z7N9
|
UHPT_CHLPN
|
Probable hexose phosphate transport protein
|
MNVWTKFFQPPKHIKEIEDQEVVKKKYKYWRIRIFYSMFIGYIFYYFTRKSFTFAMPTLIADLGFDKAQLGIIGSTLYFSYGISKFVSGVMSDQSNPRYFMAIGLMITGLTNIFFGMSSSIVLFALWWGLNGWFQGWGWPPCARLLTHWYAKSERGTWWSVWSTSHNIGGALIPILTGFIIDYSGWRGAMYVPGILCIGMGLVLINRLRDTPQSLGLPPIEKYKRDPHHAHHEGKSASEGTEEIERELSTREILFTYVLTNQWLWFLAAASFFIYIVRMAVNDWSALFLIETKHYAAVKANFCVSLFEIGGLFGMLVAGWLSDKISKGNRGPMNVLFSLGLLFAILGMWFSRSHNQWWVDGTLLFVIGFFLYGPQMMIGLAAAELSHKKAAGTASGFTGWFAYFGATFAGYPLGKVTDVWGWKGFFIALLACASIALLLFLPTWNATEKNTRSKA
|
Transport protein for sugar phosphate uptake.
|
Q9Z7P5
|
THIO_CHLPN
|
Thioredoxin (Trx)
|
MVKIISSENFDSFIASGLVLVDFFAEWCGPCRMLTPILENLAAELPHVTIGKINIDENSKPAETYEVSSIPTLILFKDGNEVARVVGLKDKEFLTNLINKHA
|
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
Q9Z7Q4
|
LPXA_CHLPN
|
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (UDP-N-acetylglucosamine acyltransferase) (EC 2.3.1.129)
|
MASIHPTAIIEPGAKIGKDVVIEPYVVIKATVTLCDNVVVKSYAYIDGNTTIGKGTTIWPSAMIGNKPQDLKYQGEKTYVTIGENCEIREFAIITSSTFEGTTVSIGNNCLIMPWAHVAHNCTIGNNVVLSNHAQLAGHVQVGDYAILGGMVGVHQFVRIGAHAMVGALSGIRRDVPPYTIGSGNPYQLAGINKVGLQRRQVPFATRLALIKAFKKIYRADGCFFESLEETLEEYGDIPEVKNFIEFCQSPSKRGIERSIDKQALEEESADKEGVLIES
|
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_00387}.
|
Q9Z7Q5
|
FMT_CHLPN
|
Methionyl-tRNA formyltransferase (EC 2.1.2.9)
|
MNLKVVYFGTPTFAATVLQDLLHHKIQITAVVTRVDKPQKRSAQLIPSPVKTIALTHGLPLLQPSKASDPQFIEELRAFNADVFIVVAYGAILRQIVLDIPRYGCYNLHAGLLPAYRGAAPIQRCIMEGATESGNTVIRMDAGMDTGDMANITRVPIGPDMTSGELADALASQGAEVLIKTLQQIESGQLQLVSQDAALATIAPKLSKEEGQVPWDKPAKEAYAHIRGVTPAPGAWTLFSFSEKAPKRLMIRKASLLAEAGRYGAPGTVVVTDRQELAIACSEGAICLHEVQVEGKGSTNSKSFLNGYPAKKLKIVFTLNN
|
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. {ECO:0000255|HAMAP-Rule:MF_00182}.
|
Q9Z7Q7
|
RL3_CHLPN
|
Large ribosomal subunit protein uL3 (50S ribosomal protein L3)
|
MRSHISVMGKKEGMIHIFDKDGSLVACSVIRVEPNVVTQIKTKESDGYFSLQIGAEEMNAPAHTITKRVSKPKLGHLRKAGGRVFRFLKEVRGSEEALNGVSLGDAFGLEVFEDVSSVDVRGISKGKGFQGVMKKFGFRGGPGSHGSGFHRHAGSIGMRSTPGRCFPGSKRPSHMGAENVTVKNLEVIKVDLEKKVLLVKGAIPGARGSIVIVKHSSRT
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
|
Q9Z7Q8
|
RL4_CHLPN
|
Large ribosomal subunit protein uL4 (50S ribosomal protein L4)
|
MVLLSKFDFSGNKIGEVEVADSLFADEGDGLQLIKDYIVAIRANKRQWSACTRNRSEVSHSTKKPFKQKGTGNARQGCLASPQFRGGGIVFGPKPKFNQHVRINRKERKAAIRLLLAQKIQTNKLTVVDDTVFVDALTAPKTQSALRFLKDCNVECRSILFIDHLDHVEKNENLRLSLRNLTAVKGFVYGININGYDLASAHNIVISKKALQELVERLVSETKD
|
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. Forms part of the polypeptide exit tunnel. {ECO:0000255|HAMAP-Rule:MF_01328}.
|
Q9Z7Q9
|
RL23_CHLPN
|
Large ribosomal subunit protein uL23 (50S ribosomal protein L23)
|
MKDPYDVIKRHYVTEKAKMLEHLSAGTGEGKKKGSFCKDPKFVFIVSHDATKPLIAQALEAIYVDKNVKVKSVNTINVKPQPARMFRGRRKGKTSGFKKAIVTFYQGHSVG
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}.
|
Q9Z7R0
|
RL2_CHLPN
|
Large ribosomal subunit protein uL2 (50S ribosomal protein L2)
|
MFKKFKPVTPGTRQLVLPAFDELTTRGELRGTKSKRSLRPNKKLSFFKKSSGGRDNLGHISCRHRGGGAKQLYRVVDFKRNKDGITAKVVTVEYDPNRSAYIALLSYEDGEKRYILAPKGIQRGDVVVSGEGSPFKPGCCMTLKSIPLGLSVHNIEMRPSSGGKLVRSAGLAAQVIAKSPGYVTLKMPSGEFRMLNEGCRATIGEVSNADHNLRVDGKAGRRRWMGVRPTVRGTAMNPVDHPHGGGEGRHNGYIPRTPWGKVTKGLKTRDKNKSNKWIVKDRRK
|
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
|
Q9Z7R1
|
RS19_CHLPN
|
Small ribosomal subunit protein uS19 (30S ribosomal protein S19)
|
MSRSLRKGPFVDHHLLKKVRAMNIEEKKTPIKTWSRRSMITPEMIGHTFEVHNGKKFLTVFVSETMVGHKLGEFSPTRIFKSHPVKKG
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q9Z7R2
|
RL22_CHLPN
|
Large ribosomal subunit protein uL22 (50S ribosomal protein L22)
|
MFKATARYIRVQPRKARLAAGLMRNLSVQEAEEQLGFSQLKAGRCLKKVLNSAVANAELHENIKRENLSVTEVRVDAGPVYKRSKSKSRGGRSPILKRTSHLTVIVGEKER
|
This protein binds specifically to 23S rRNA its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). {ECO:0000255|HAMAP-Rule:MF_01331}. The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
|
Q9Z7R3
|
RS3_CHLPN
|
Small ribosomal subunit protein uS3 (30S ribosomal protein S3)
|
MGQKGCPIGFRTGVTKKWRSLWYGNKQEFGKFLIEDVRIRQFLRKKPSCQGAAGFVVRRMSGKIEVTIQTARPGLVIGKKGAEVDLLKEELRALTGKEVWLEIAEIKRPELNAKLVADNIARQIERRVSFRRAMKKAMQSVMDAGAVGVKIQVSGRLAGAEIARSEWYKNGRVPLHTLRADIDYATACAETTYGIIGIKVWINLGENSSSTTPNNPAAPSAAA
|
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-Rule:MF_01309}.
|
Q9Z7R4
|
RL16_CHLPN
|
Large ribosomal subunit protein uL16 (50S ribosomal protein L16)
|
MLMPKRTKFRKQQKGQFAGLSKGATFVDFGEYAMQTLERGWVTSRQIEACRVAINRYLKRRGKVWIRIFPDKSVTKKPAETRMGKGKGAPDHWVAVVRPGRILFEVANVSKEDAQDALRRAAAKLGIKTRFVKRVERV
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. {ECO:0000255|HAMAP-Rule:MF_01342}.
|
Q9Z7R6
|
RS17_CHLPN
|
Small ribosomal subunit protein uS17 (30S ribosomal protein S17)
|
MASEPRGSRKVKIGVVVSAKMEKTVVVRVERIFSHPQYLKVVRSSKKYYAHTELKVSEGDKVKIQETRPLSKLKRWRVIEHVGVVS
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_01345}.
|
Q9Z7R7
|
RL14_CHLPN
|
Large ribosomal subunit protein uL14 (50S ribosomal protein L14)
|
MIQQESQLKVADNTGAKKVKCFKVLGGSRRRYATVGDVIVCSVRDVEPNSSIKKGDVIKAVIVRTRRHITRKDGSTLKFDTNSCVIIDDKGNPKGTRIFGPVAREIRDRGFIKISSLAPEVI
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}.
|
Q9Z7R8
|
RL24_CHLPN
|
Large ribosomal subunit protein uL24 (50S ribosomal protein L24)
|
MKKQNIRVGDKVFILAGNDKGKEGKVLSLTEDKVVVEGVNVRIKNIKRSQQNPKGKRISIEAPIHISNVRLTIAGEPAKLSVKVTEQGRELWQRRPDGTSQLYRLVRGKKG
|
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. {ECO:0000255|HAMAP-Rule:MF_01326}.
|
Q9Z7R9
|
RL5_CHLPN
|
Large ribosomal subunit protein uL5 (50S ribosomal protein L5)
|
MSRLKKFYTEEIRKSLFEKFGYANKMQIPVLKKIVLSMGLAEAAKDKNLFQAHLEELTMISGQKPLVTKARNSIAGFKLREGQGIGAKVTLRGIRMYDFMDRFCNIVSPRIRDFRGFSNKGDGRGCYSVGLDDQQIFPEINLDRVKRTQGLNITWVTTAQTDDECTTLLELMGLRFKKAQ
|
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits this bridge is implicated in subunit movement. Contacts the P site tRNA the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-Rule:MF_01333}.
|
Q9Z7S0
|
RS8_CHLPN
|
Small ribosomal subunit protein uS8 (30S ribosomal protein S8)
|
MGMTSDSIADLLTRIRNALMAEHLYVDVEHSKMREAIVKILKHKGFVAHYLVKEENRKRAMRVFLQYSDDRKPVIHQLKRVSKPSRRVYVSAAKIPYVFGNMGISVLSTSQGVMEGSLARSKNIGGELLCLVW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01302}.
|
Q9Z7S1
|
RL6_CHLPN
|
Large ribosomal subunit protein uL6 (50S ribosomal protein L6)
|
MSRKAREPILLPQGVEVSIQDDKIIVKGPKGSLTQKSVKEVEITLKDNSIFVHAAPHVVDRPSCMQGLYWALISNMVQGVHLGFEKRLEMIGVGFRASVQGAFLDLSIGVSHPTKIPIPSTLQVSVEKNTLISVKGLDKQLVGEFAASIRAKRPPEPYKGKGIRYENEYVRRKAGKAAKTGKK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}.
|
Q9Z7S2
|
RL18_CHLPN
|
Large ribosomal subunit protein uL18 (50S ribosomal protein L18)
|
MESSLCKKSLMKRRRALRVRKVLKGSPTKPRLSVVKTNKHIYVQLIDDSIGKTLASVSTLSKLNKSQGLTKKNQEVAKVLGTQIAELGKNLQLDRVVFDRGPFKYHGIVSMVADGAREGGLQF
|
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01337}.
|
Q9Z7S3
|
RS5_CHLPN
|
Small ribosomal subunit protein uS5 (30S ribosomal protein S5)
|
MSLSKNSHKEDQLEEKVLVVNRCSKVVKGGRKFSFSALILVGDGKGRLGYGFAKANELTDAIRKGGEAAKKNLMKIEALEDGSIPHEVLVHHDGAQLLLKPAKPGTGIVAGSRIRLILEMAGIKDIVAKSFGSNNPMNQVKAAFKALTGLSPRKDLLRRGAAIND
|
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}.
|
Q9Z7S4
|
RL15_CHLPN
|
Large ribosomal subunit protein uL15 (50S ribosomal protein L15)
|
MIKLESLFDISERKRRKKLLGRGPSSGHGKTSGRGHKGDGSRSGYKRRFGYEGGGVPLYRRVPTRGFSHKRFDKCVEEITTGRLAELFQEGEAITLDALKAKKAIARQAVRVKVILKGDLEKTFVWQDTAVVLSQGVQNLLGIT
|
Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01341}.
|
Q9Z7S5
|
SECY_CHLPN
|
Protein translocase subunit SecY
|
MTTLRQFFLITELRQKLFYTFALLTACRVGVFIPVPGINGELAVAYFKQLLGSGQNLFQLADIFSGGAFAQMTVIALGVVPYISASIIVQLFLVFMPALQREMRESSDQGKRRIGRLTRLFTVALAVIQSLLFAKFALRMNLTIPGIVLPTLLSSKLFGVPWIFYITTVVVMTTGTLLLMWIGEQISDKGIGNGISLIIALGILSSFPSVLGSIVNKLNLGSQDSSDLGLISILILALVFVFVLITTILIIEGVRKIPVQYARRVIGRREVPGGGSYLPLKVNYAGVIPVIFASSLLMFPATIGQFIASESSWMKRIAALLAPGSLVYSICYVLLIIFFTYFWTATQFHPEQIASEMKKNNAFIPGIRQGKPTQHYLEYTMNRVTLLGALFLAAIAILPSLLGCLLRVDSNVSYFLGGTAMLIVVGVVLDTMKQVDAFLLMRRYDSVLKTDRTKGRH
|
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}.
|
Q9Z7S7
|
RS11_CHLPN
|
Small ribosomal subunit protein uS11 (30S ribosomal protein S11)
|
MVKNQAQAKKSVKRKQLKNIPSGVVHVKATFNNTIVSITDPAGNVISWASAGKVGYSGSRKSSAFAATVAAQDAAKTAMNSGLKEVEVCLKGTGAGRESAVRALISAGLVVSVIRDETPVPHNGCRPRKRRRV
|
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}.
|
Q9Z7T4
|
RUVA_CHLPN
|
Holliday junction branch migration complex subunit RuvA
|
MYDYIRGTLTYVHTGAIVIECQGIGYHIAITERWAIECIRALHQDFLVFTHVIFRETEHLLYGFHSREERECFRILISFSGIGPKLALAILNALPLKVLCSVVRSEDIRALASVSGIGKKTAEKLMVELKQKLPDLLPLDSRVETSQTHTTSSCLEEGIQALAALGYSKIAAERMIAEAIKDLPEGSSLTDILPIALKKNFSGVNKD
|
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}.
|
Q9Z7T7
|
MNMG_CHLPN
|
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG (Glucose-inhibited division protein A)
|
MWTHPIAYDVIVVGAGHAGCEAAYCSAKMGVSVLMLTSNLDTIAKLSCNPAVGGIGKGHIVREIDALGGIMAEVTDQSGIQFRILNQTKGPAVRAPRAQVDKQLYHIHMKRLLENTPGLHIMQATVESLLDKEGVISGVTTKEGWMFSGKTVVLSSGTFMRGLIHIGDRNFSGGRLGDPSSQGLSEDLKKRGFPISRLKTGTPPRLLASSINFSCMEEQPGDLGVGFVHRTEPFQPPLPQLSCFITHTMEKTKAIISANLHRSALYGGCIEGVGPRYCPSIEDKIVKFSDKERHHVFLEPEGLHTQEIYANGLSTSMPFDVQYDMIRSVLGLENAIITRPAYAIEYDYIHGNVIHPTLESKLIEGLFLCGQINGTTGYEEAAAQGLIAGINAVNKVFNRPPFIPSRQESYIGVMLDDLTTQILDEPYRMFTGRAEHRLLLRQDNACARLSHYGYELGLLSEERYELVKKQNQLLEEEKVRLQKTFRQYGQSVVSLAKALSRPEVSYDMLREAFPNDIRDLGAVLNASLEMEIKYSGYIDRQKILIQSLEKAESLLIPEDLDYKQITALSLEAQEKLAKFTPRTLGSASRISGIASADIQVLMIALKKHAHH
|
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}.
|
Q9Z7W5
|
RECO_CHLPN
|
DNA repair protein RecO (Recombination protein O)
|
MQICVTGVVLRSRPLGKNHTLTTLFTPEGLFTFFAKQGQTLQCDYRETLVPISLGKYTLHRNGSRLPKLTHGDILNAFEAIKQTYALLEASGKMIQALLASQWKEKPSHKLFSLFLNFLHRIPESSNPEFFAAIFVLKLLQYEGILDLTPACSLCKASLPYACYRYQGHKLCKKHQHKQAISIEKEEEQILQAIIHAKQFSELLAIAEFPIAIAEKIFYLFDSLQEEKKSERNSSEDPYHEILRLSKVVHPY
|
Involved in DNA repair and RecF pathway recombination.
|
Q9Z7X5
|
ISPD_CHLPN
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60) (4-diphosphocytidyl-2C-methyl-D-erythritol synthase) (MEP cytidylyltransferase) (MCT)
|
MIKSSLILLSGGQGTRFGSKIPKQYLPLNGTPLVLHSLKILSSLPQIAEVIVVCDPSYQETFQEYPVSFAIPGERRQDSVFSGLQQVSYPWVIIHDGARPFIYPDEIHDLLETAEKIGATALASPIPYTIKQRNPVRTLDRDNLAIIHTPQCIKTEILREGLALAKEKQLTLVDDIEAAEIIGKPSQLVFNKHPQIKISYPEDLTIAQALL
|
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q9Z7Y7
|
ISPT_CHLPN
|
Isoprenyl transferase (EC 2.5.1.-)
|
MSLATNNAESKFPSLQRLPNHVAIIMDGNRRWYKKHREECGHTHTSGHYYGAKVLPNILNAVLDLGIKVLTLYTFSTENFGRPKEEIQEIFNIFYTQLDKQLPYLMENEICLRCIGDLSKLPKGIQTKINHVSRMTASFSRLELVLAVNYGGKDELVRAFKKLHVDILNKKISSDDLSESLISSYLDTSGLTDPDLLIRTGGEMRVSNFLLWQIAYTELYITDTLWPDFTPQDLFEAINVYQQRSRRGGK
|
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. {ECO:0000255|HAMAP-Rule:MF_01139}.
|
Q9Z801
|
RS7_CHLPN
|
Small ribosomal subunit protein uS7 (30S ribosomal protein S7)
|
MSRRHSAEKRDIPGDPIYGSVILEKFINKVMMHGKKSVARKIVYSALERFGKKLNLENVLEGFGEALENAKPILEVRSRRVGGATYQVPVEVASERRNCLAMQWIIKHARSKPGKSMEVGLATELIDCFNKQGATIKKREDTHRMAEANKAFAHYKW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. {ECO:0000255|HAMAP-Rule:MF_00480}.
|
Q9Z802
|
EFG_CHLPN
|
Elongation factor G (EF-G)
|
MSNQEFDLSAIRNIGIMAHIDAGKTTTTERILFYAGRTHKIGEVHEGGATMDWMAQEQERGITITSAATTVFWLGAKINIIDTPGHVDFTIEVERSLRVLDGAVAVFDAVSGVEPQSETVWRQADKYGVPRIAFVNKMDRMGADYFAAVESMKEKLGANAFPVHCPIGSESQFVGMVDLISQKALYFLDDTLGAKWEEKEISEDLKERCAELRANLLEELATIDESNEAFMMKVLEDPDSITEDEIHQVMRKGVIENKINPVLCGTAFKNKGVQQLLNVIVKWLPSPLDRGNIRGINLKTDQEISLEPRRDGPLAALAFKIMTDPYVGRITFIRIYSGTLKKGSAILNSTKDKKERISRLLEMHANERTDRDEFTVGDIGACVGLKFSVTGDTLCDDNQEIVLERIEFPDPVIDMAIEPKSKGDREKLAQALSSLSEEDPTFRVSTNEETGQTIISGMGELHLDILRDRMIREFKVEANVGKPQVSYKETITVSGNSETKYVKQSGGRGQYAHVCLEIEPNEPGKGNEVVSKIVGGVIPKEYIPAVIKGIEEGLNTGVLAGYGLVDVKVSIVFGSYHEVDSSEMAFKICGSMAVKDACRKAKPVILEPIMKVAVITPEDHLGDVIGDLNRRRGKILGQESSRGMAQVNAEVPLSEMFGYTTSLRSLTSGRATSTMEPAFFAKVPQKIQEEIVKK
|
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
|
Q9Z803
|
RS10_CHLPN
|
Small ribosomal subunit protein uS10 (30S ribosomal protein S10)
|
MKQQKQKIRIRLKGFDQGQLDRSTADIVETAKRTGARVVGPIPLPTKREVYTVLRSPHVDKKSREQFEIRTHKRLVDILDPTGKTIDALKMLALPAGVDIKIKAA
|
Involved in the binding of tRNA to the ribosomes. {ECO:0000255|HAMAP-Rule:MF_00508}.
|
Q9Z806
|
RL21_CHLPN
|
Large ribosomal subunit protein bL21 (50S ribosomal protein L21)
|
MEPYAVIQTGSKQYQVRSGDVIDVELLGEVASDKEVIFQDVLFVFDGTKASLGSPTIANAQVKAEYLSHVKGEKVVAYKYKKRKNYHRKHGHRQKYLRVKIREILI
|
This protein binds to 23S rRNA in the presence of protein L20. {ECO:0000255|HAMAP-Rule:MF_01363}.
|
Q9Z809
|
Y543_CHLPN
|
Probable metal transport system membrane protein CPn_0543/CP_0209/CPj0543/CpB0565
|
MLSSLIRDSFPLLILLPTFLAALGASVAGGVMGTYIVVKRIVSISGSISHAILGGIGLTLWIQYKLHLSFFPMYGAIVGAIFLALCIGKIHLKYQEREDSLIAMIWSVGMAIGIIFISRLPTFNGELINFLFGNILWVTPSDLYSLGIFDLLVLGIVVLCHTRFLALCFDERYTALNHCSVQLWYFLLLVLTAITIVMLIYVMGTILMLSMLVLPVAIACRFSYKMTRIMFISVLLNILCSFSGICIAYCLDFPVGPTISLLMGLGYTASLCVKKRYNPSTPSPVSPEINTNV
|
Part of an ATP-driven transport system CPn_0541/CPn_0542/CPn_0543 for a metal.
|
Q9Z810
|
Y542_CHLPN
|
Probable metal transport system ATP-binding protein CPn_0542/CP_0210/CPj0542/CpB0563
|
MTIRILAEGLAFRYGSKGPNIIHDVSFSVYDGDFIGIIGPNGGGKSTLTMLILGLLTPTFGSLKTFPSHSAGKQTHSMIGWVPQHFSYDPCFPISVKDVVLSGRLSQLSWHGKYKKKDFEAVDHALDLVGLSDHHHHCFAHLSGGQIQRVLLARALASYPEILILDEPTTNIDPDNQQRILSILKKLNRTCTILMVTHDLHHTTNYFNKVFYMNKTLTSLADTSTLTDQFCCHPYKNQEFSCSPH
|
Part of an ATP-driven transport system CPn0541/CPn0542/CPn0543 for a metal. Probably responsible for energy coupling to the transport system.
|
Q9Z811
|
Y541_CHLPN
|
Putative metal-binding protein CP_0211
|
MHKVIVFIFLTLYSLKSYGNDVIDKPHVLVSIAPYKFLVEQIAEETCFVYAIVTNHYDPHTYELPPQQIKELRQGDLWFRIGEAFEKTCERNLTCQQVDLSQNVSLIQGKPCCNQHTTNYDTHTWLSPKNLKVQVETIVTTLSKKYPQHATLYQSNGEKLLLALDQLNEEILTITSKAKQRHILVSHGAFGYFCRDYNFSQHTIEKSSHVEPSPKDVARVFRDIEQYKISSVILLEYSGRRSSAMLADRFHMHTVNLDPYAENVLVNLKTIATTFSSL
|
Part of an ATP-binding cassette (ABC) transport system involved in metal import (By similarity). Binds a metal with high affinity and specificity and delivers it to the membrane permease for translocation into the cytoplasm (By similarity).
|
Q9Z819
|
NRDR_CHLPN
|
Transcriptional repressor NrdR
|
MQCPFCNHGELKVIDSRNAPEANAIKRRRECLKCSQRFTTFETVELTLQVLKRDGRYENFQESKLIHGLNAASSHTRIGQDQVHAIASNVKSELLGKQNREISTKEIGELVMKYLKKADMIAYIRFACVYRRFKDVGELMEVLLSATPDMEK
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes. {ECO:0000255|HAMAP-Rule:MF_00440}.
|
Q9Z820
|
RISA_CHLPN
|
Riboflavin synthase (RS) (EC 2.5.1.9)
|
MFSGIIQELGEVCFFEAQGNGLSLGIKSTPLFVTPLVTGDSVAVDGVCLTLTSCNESKIFFDVIPETLACTTLGEKRCSDQVNLEAALKMGDSIGGHLLSGHVFGTAEIFLIKENRYYFRGSKELSQYLFEKGFIAIDGISLTLVSVDSDTFSVGLIPETLQRTTLGKKREGERVNIEIDMSTKIQVDTVKRILASSGKD
|
Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
|
Q9Z823
|
LPXK_CHLPN
|
Tetraacyldisaccharide 4'-kinase (EC 2.7.1.130) (Lipid A 4'-kinase)
|
MKKRFPSTLFLFYRRVTIAISLEGILGWGWLGSLLSKVFAFLVACWNRFSWSTPYRARSTVISVGNIVVGGAGKTPTVLWLAEALRLRGYSCGVLSRGYKSQSSRQKKLTVVDSKVHSASYVGDEPLLMAEKLPEGSVWVHKDRRISAARAAEKFGILLLDDGLQYRKLHKDVEIAVVNGQDPLGGRAFFPKGRLRDFPLRLKTVDAIIVNGGGKEAGTVVKRVSNAPQIFVKPTIASVVWTHNGERIPKEALRELRVGVFCGLGFPQGFLNMLREEGIHILGKYLLPDHAAITKKELNYFCQQMAMRQGQGLLCTEKDSVKLPRLSGEVSLLPIAKVEMRLSVNQDDTLSLLNMIEQIHKNRGN
|
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}.
|
Q9Z843
|
YBEY_CHLPN
|
Endoribonuclease YbeY (EC 3.1.-.-)
|
MTQEKIKIHVSNEQTCIPIHLVSVEKLVLTLLEHLKVTTNEIFIYFLEDKALAELHDKVFADPSLTDTITLPIDAPGDPAYPHVLGEAFISPQAALRFLENTSPNQEDIYEEISRYLVHSILHMLGYDDTSSEEKRKMRVKENQILCMLRKKHALLTA
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00009}.
|
Q9Z849
|
GRPE_CHLPN
|
Protein GrpE (HSP-70 cofactor)
|
MTDTPPENEEQHESNVQNENEVEHLQQEIVTLKTELKEKNDKYLMALAESENSRKRLQKERQELMQYALENTLIDFLNPIESMEKALGFATQMSDDVKNWALGFNMILNQFKQIFEEKGIIEYSSIGQKFNPFLHEAVQTEETSEVPEGTILEEFAKGYKIGERPIRVAKVKVAKAPTPKENKE
|
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}.
|
Q9Z850
|
HRCA_CHLPN
|
Heat-inducible transcription repressor HrcA
|
MLSVTIVLVGLEMARSKVSKRDSKILDILFATTELYLKTGQPVGSKTLKESFCSDLSTATIRNYFAELEAEGFLKKNHTSGGRIPTDLALRHYVDHQEECPEAEISAPIFDKISQLPSESRNIIKDLQKATELLGEILDLPTFFSSPRFENDSVTNIQITQVDKQRAVTILSTEFGQIFTDTLWLPEACDTLSIKRIEKFLQNYIRKLPTNEELSKKEEHLSMSLYNEVVVRYLTRYCNFSEEDLYQTGMSKLLKYEAFKDPEVLALGLSLFENRRQMCELLNIGMHKGRATAFIGKELSDILGTSNPGCSVITIPYYMNRSPLGALGILGPINLPYKEALPLLKLFANKINETLTQSFYKFKLSFRRPLTSNCKLSNEPILRTEYSSIKLLPSKETL
|
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. {ECO:0000255|HAMAP-Rule:MF_00081}.
|
Q9Z851
|
SYP_CHLPN
|
Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)
|
MKTSQLFYKTSKNANKSAAVLSNELLEKAGYLFKVSKGVYTYTPLLWRVVSKMMNIIREELNAIGGQELLLPLLHNAELWQHTGRWEAFTSEGLLYTLKDREGKSHCLAPTHEEVICSFVAQWLSSKRQLPLHLYQIATKFRDEIRPRFGLIRSRELLMEDSYTFSDSPEQMNEQYEKLRSAYSKIFDRLGLAYVIVTADGGKIGKGKSEEFQVLCSLGEDTICVSGSYGANIEAAVSIPPQHAYDREFLPVEEVATPGITTIEALANFFSIPLHKILKTLVVKLSYSNEEKFIAIGMRGDRQVNLVKVASKLNADDIALASDEEIERVLGTEKGFIGPLNCPIDFFADETTSPMTNFVCAGNAKDKHYVNVNWDRDLLPPQYGDFLLAEEGDTCPENPGHPYRIYQGIEVAHIFNLGTRYTDSFEVNFQDEHGQTQQCWMGTYGIGVGRTLAACVEQLADDRGIVWPKALAPFSITIAFNGGDTVSQELAETIYHELQSQGYEPLLDDRDERLGFKLKDSDLIGIPYKLILGKSYQSSGIFEIESRSGEKYTVSPEAFPTWCQNHLA
|
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}.
|
Q9Z8B9
|
DNAA2_CHLPN
|
Chromosomal replication initiator protein DnaA 2
|
MLTCNECTTWEQFLNYVKTRCSKTAFENWISPIQVLEETQEKIRLEVPNIFVQNYLLDNYKRDLCSFVPLDVHGEPALEFVVAEHKKPSAPVASQKESNEGISEVFEETKDFELKLNLSYRFDNFIEGPSNQFVKSAAVGIAGKPGRSYNPLFIHGGVGLGKTHLLHAVGHYVREHHKNLRIHCITTEAFINDLVYHLKSKSVDKMKNFYRSLDLLLVDDIQFLQNRQNFEEEFCNTFETLINLSKQIVITSDKPPSQLKLSERIIARMEWGLVAHVGIPDLETRVAILQHKAEQKGLLIPNEMAFYIADHIYGNVRQLEGAINKLTAYCRLFGKSLTETTVRETLKELFRSPTKQKISVETILKSVATVFQVKLNDLKGNSRSKDLVLARQIAMYLAKTLITDSLVAIGAAFGKTHSTVLYACKTIEHKLQNDETLKRQVNLCKNHIVG
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity).
|
Q9Z8C2
|
RSMH_CHLPN
|
Ribosomal RNA small subunit methyltransferase H (EC 2.1.1.199) (16S rRNA m(4)C1402 methyltransferase) (rRNA (cytosine-N(4)-)-methyltransferase RsmH)
|
MSERAHIPVLVEECLALFAQRPPQTFRDVTLGAGGHAYAFLEAYPSLTCYDGSDRDLQALAIAEKRLETFQDRVSFSHASFEDLANQPTPRLYDGVLADLGVSSMQLDTLSRGFSFQGEKEELDMRMDQTQELSASDVLNSLKEEELGRIFREYGEEPQWKSAAKAVVHFRKHKKILSIQDVKEALLGVFPHYRFHRKIHPLTLIFQALRVYVNGEDRQLKSLLTSAISWLAPQGRLVIISFCSSEDRPVKWFFKEAEASGLGKVITKKVIQPTYQEVRRNPRSRSAKLRCFEKASQ
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01007}.
|
Q9Z8C7
|
DBH_CHLPN
|
Probable DNA-binding protein HU
|
MATMTKKKLISTISQDHKIHPNHVRTVIQNFLDKMTDALVKGDRLEFRDFGVLQVVERKPKVGRNPKNAAVPIHIPARRAVKFTPGKRMKRLIETPNKHS
|
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
|
Q9Z8F9
|
HCT2_CHLPN
|
Histone H1-like protein HC2 (HC2 nucleoprotein)
|
MIGAQKKQSGKKTASRAVRKPAKKVAAKRTVKKATVRKTAVKKPAVRKTAAKKTVAKKTTAKRTVRKTVAKKPAVKKVAAKRVVKKTVAKKTTAKRAVRKTVAKKPVARKTTVAKGSPKKAAACALACHKNHKHTSSCKRVCSSTATRKHGSKSRVRTAHGWRHQLIKMMSR
|
Might have a role in establishing the nucleoid structure of elementary bodies.
|
Q9Z8J4
|
YTGA_CHLPN
|
Metal-binding protein YtgA
|
MDAKMGYIFKVMRWIFCFVACGITFGCTNSGFQNANSRPCILSMNRMIHDCVERVVGNRLATAVLIKGSLDPHAYEMVKGDKDKIAGSAVIFCNGLGLEHTLSLRKHLENNPNSVKLGERLIARGAFVPLEEDGICDPHIWMDLSIWKEAVIEITEVLIEKFPEWSAEFKANSEELVCEMSILDSWAKQCLSTIPENLRYLVSGHNAFSYFTRRYLATPEEVASGAWRSRCISPEGLSPEAQISVRDIMAVVDYINEHDVSVVFPEDTLNQDALKKIVSSLKKSHLVRLAQKPLYSDNVDDNYFSTFKHNVCLITEELGGVALECQR
|
Part of the ATP-binding cassette (ABC) transport system YtgABCD involved in metal import. Binds Fe(2+), Mn(2+) and Ni(2+), with a preference for Fe(2+) and delivers them to the membrane permease for translocation into the cytoplasm.
|
Q9Z8J5
|
Y348_CHLPN
|
Probable metal transport system ATP-binding protein CPn_0348/CP_0412/CPj0348/CpB0355
|
MNVKDETFWSVHNLCVNYEHAAVLYHISFSLGKGSLTAILGPNGAGKSTLLKASLGLIKPSSGTVYFFNQKFKKVRQRIAYMPQRASVDWDFPMTVLDLALMGCYSYKGMWGRISSDDRREAFHILERVGLESVADRQIGQLSGGQQQRAFLARALMQKADLYLMDELFSAIDMASFKTSVGVLQELRDQGKTIVVVHHDLSHVRQLFDHVVLLNKRLICCGPTDECLNGDTIFQTYGCEIELLEQTLKLSRGKQFGSC
|
Part of an ATP-driven transport system CPn0346/CPn0347/CPn0348/CPn0349 for a metal. Probably responsible for energy coupling to the transport system.
|
Q9Z8J6
|
Y347_CHLPN
|
Probable metal transport system membrane protein CPn_0347/CP_0413/CPj0347/CpB0354
|
MLSCVFSDTIFLSSFLAVTLICMTTALWGTILLISKQPLLSESLSHASYPGLLVGALMAQYVFSLQASIFWIVLFGCAASVFGYGIIVFLGKVCKLHKDSALCFVLVVFFAIGVILASYVKESSPTLYNRINAYLYGQAATLGFLEATLAAIVFCASLFALWWWYRQIVVTTFDKDFAVTCGLKTVLYEALSLIFISLVIVSGVRSVGIVLISAMFVAPSLGARQLSDRLSTILILSAFFGGISGALGSYISVAFTCRAIIGQQAVPVTLPTGPLVVICAGLLAGLCLLFSPKSGWVIRFVRRKHFSFSKDQEHLLKVFWHISHNRLENISVRDFVCSYKYQEYFGPKPFPRWRVQILEWRGYVKKEQDYYRLTKKGRSEALRLVRAHRLWESYLVNSLDFSKESVHELAEEIEHVLTEELDHTLTEILNDPCYDPHRQIIPNKKKEV
|
Part of an ATP-driven transport system CPn_0346/CPn_0347/CPn_0348/CPn_0349 for a metal.
|
Q9Z8J7
|
Y346_CHLPN
|
Probable metal transport system membrane protein CPn_0346/CP_0414/CPj0346/CpB0353
|
MALGPSPYYGVSFFQFFSVFFSRLFSGSLFTGSLYIDDIQIIVFLAISCSGAFAGTFLVLRKMAMYANAVSHTVLFGLVCVCLFTHQLTTLSLGTLTLAAMATAMLTGFLIYFIRNTFKVSEESSTALVFSLLFSLSLVLLVFMTKNAHIGTELVLGNADSLTKEDIFPVTIVILANAVITIFAFRSLVCSSFDSVFASSLGIPIRLVDYLIIFQLSACLVGAFKAVGVLMALAFLIIPSLIAKVIAKSIRSLMAWSLVFSIGTAFLAPASSRAILSAYDLGLSTSGISVVFLTMMYIVVKFISYFRGYFSKNFEKISEKSSQY
|
Part of an ATP-driven transport system CPn_0346/CPn_0347/CPn_0348/CPn_0349 for a metal.
|
Q9Z8K0
|
DPO3B_CHLPN
|
Beta sliding clamp (Beta clamp) (Sliding clamp) (Beta-clamp processivity factor) (DNA polymerase III beta sliding clamp subunit) (DNA polymerase III subunit beta)
|
MKFVVSRNELGNLIKKIQSVVPQNTPIPVLTHVLIETYNDELVFTATDLTVSTRCVTKAKVYEKGAISIPSKRFFQLVKELTEANLEISSSAGEMAQITSGSSCFRLLSMEKEDFPMLPDIQNALRFSLPAEQLKTMLQRTSFAVSREESRYVLTGVLLAIANGVATIVGTDGKRLAKIDAEVTLDKSFSGEYIIPIKAVEEIIKMCSDEGEATIFLDQDKIAVECDNTLLITKLLSGEFPDFSPVISTESNVKLDLHREELITLLKQVALFTNESSHSVKFSFLPGELTLTANCTKVGEGKVSMAVNYSGELLEIAFNPFFFLDILKHSKDELVSLGISDSYNPGIITDSASGLFVIMPMRLHDD
|
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.
|
Q9Z8K1
|
SSRP_CHLPN
|
SsrA-binding protein (Small protein B)
|
MAQKEIVSNRKALRNYEVIETLEAGIVLTGTEIKSLRDHGGNLGDAYVIVSKGEGWLLNASIAPYRFGNIYNHEERRKRKLLLHRYELRKLEGKIAQKGMTLIPLGMFLSRGYVKVRLGCCRGKKAYDKRRTIIEREKEREVAAAMKRRHH
|
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation. {ECO:0000255|HAMAP-Rule:MF_00023}.
|
Q9Z8L9
|
TRUB_CHLPN
|
tRNA pseudouridine synthase B (EC 5.4.99.25) (tRNA pseudouridine(55) synthase) (Psi55 synthase) (tRNA pseudouridylate synthase) (tRNA-uridine isomerase)
|
MDLAVELKEGILLVDKPQGRTSFSLIRALTKLIGVKKIGHAGTLDPFATGVMVMLIGRKFTRLSDILLFEDKEYEAIAHLGTTTDSYDCDGKVVGRSKKIPSLEEVLSAAEYFQGEIQQLPPMFSAKKVQGKKLYEYARKGLSIERHHSTVQVHLQITKYEYPLLHFVVSCSKGTYIRSIAHELGTMLGCGAYLEQLRRLRSGRFSIDECIDGNLLDHPDFDISPYLRDAHGNSL
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01080}.
|
Q9Z8M0
|
RBFA_CHLPN
|
Ribosome-binding factor A
|
MTENRRIKRVNALLQEAIAKVILKDVKHPKISNLWITVTRVSLSKDLHSARVYVSVMPHENTKEEALEALKVSAGFIAHRASKNVVLKYFPELHFYLDDIFSPQDYIENLLWQIQEKEKS
|
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}.
|
Q9Z8M3
|
RS1_CHLPN
|
Small ribosomal subunit protein bS1 (30S ribosomal protein S1)
|
MPKQAEYTWGSKKILDNIECLTEDVAEFKDLLYTAHRITSSEEESDNEIQPGAILKGTVVDINKDFVVVDVGLKSEGVIPMSEFIDSSEGLVLGAEVEVYLDQAEDEEGKVVLSREKATRQRQWEYILAHCEEGSIVKGQITRKVKGGLIVDIGMEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKINVERRNIVVSRRELLEAERISKKAELIEQISIGEYRKGVVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKEHNPWEDIEKKYPPGKRVLGKIVKLLPYGAFIEIEEGIEGLIHISEMSWVKNIVDPSEVVNKGDEVEAIVLSIQKDEGKISLGLKQTERNPWDNIEEKYPIGLHVNAEIKNLTNYGAFVELEPGIEGLIHISDMSWIKKVSHPSELFKKGNSVEAVILSVDKESKKITLGVKQLSSNPWNEIEAMFPAGTVISGVVTKITAFGAFVELQNGIEGLIHVSELSDKPFAKIEDIISIGENVSAKVIKLDPDHKKVSLSVKEYLADNAYDQDSRTELDFKDSQGPKERKKKGK
|
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).
|
Q9Z8M5
|
ACPS_CHLPN
|
Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase AcpS)
|
MEIIHIGTDIIEISRIREAIATHGNRLLNRIFTEAEQKYCLEKTDPIPSFAGRFAGKEAVAKALGTGIGSVVAWKDIEVFKVSHGPEVLLPSHVYAKIGISKVILSISHCKEYATATAIALA
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP-Rule:MF_00101}.
|
Q9Z8M9
|
DNAA1_CHLPN
|
Chromosomal replication initiator protein DnaA 1
|
MRAWEEFLLLQEKEIGTNTVDKWLRSLKVLCFDACNLYLEAQDSFQITWFEEHIRHKVKSGLVNNNNKPIRVHVTSVDKAAPFYKEKQMQQEKTAYFTMHYGSVNPEMTFSNFLVTPENDLPFRVLQEFTKSPDENGGVTFNPIYLFGPEGSGKTHLMQSAISVLRESGGKILYVSSDLFTEHLVSAIRSGEMQKFRSFYRNIDALFIEDIEVFSGKSATQEEFFHTFNSLHSEGKLIVVSSSYAPVDLVAVEDRLISRFEWGVAIPIHPLVQEGLRSFLMRQVERLSIRIQETALDFLIYALSSNVKTLLHALNLLAKRVMYKKLSHQLLYEDDVKTLLKDVLEAAGSVRLTPLKIIRNVAQYYGVSQESILGRSQSREYVLPRQVAMYFCRQKLSLSYVRIGDVFSRDHSTVISSIRLIEQKIEENSHDIHMAIQDISKNLNSLHKSLEFFPSEEMII
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity).
|
Q9Z8N1
|
PHSG_CHLPN
|
Glycogen phosphorylase (EC 2.4.1.1)
|
MEDFSSFDKNKVSVDSMKRAILDRLYLSVVQSPESASPRDIFTAVAKTVMEWLAKGWLKTQNGYYKNDVKRVYYLSMEFLLGRSLKSNLLNLGILDLVRKALKTLNYDFDHLVEMESDAGLGNGGLGRLAACYLDSMATLAVPAYGYGIRYDYGIFDQRIVNGYQEEAPDEWLRYGNPWEICRGEYLYPVRFYGRVIHYTDSRGKQVADLVDTQEVLAMAYDIPIPGYGNDTVNSLRLWQAQSPRGFEFSYFNHGNYIQAIEDIALIENISRVLYPNDSITEGQELRLKQEYFLVSATIQDIIRRYTKTHICLDNLADKVVVQLNDTHPALGIAEMMHILVDREELPWDKAWEMTTVIFNYTNHTILPEALERWPLDLFSKLLPRHLEIIYEINSRWLEKVGSRYPKNDDKRRSLSIVEEGYQKRINMANLAVVGSAKVNGVSSFHSQLIKDTLFKEFYEFFPEKFINVTNGVTPRRWIALCNPRLSKLLNETIGDRYIIDLSHLSLIRSFAEDSGFRDHWKGVKLKNKQDLTSRIYNEVGEIVDPNSLFDCHIKRIHEYKRQLMNILRVIYVYNDLKENPNQDVVPTTVIFSGKAAPGYVMAKLIIKLINSVADVVNQDSRVNDKLKVLFLPNYRVSMAEHIIPGTDLSEQISTAGMEASGTGNMKFALNGALTIGTMDGANIEMAEHIGKENMFIFGLLEEQIVQLRREYCPQTICDKNPKIRQVLDLLEQGFFNSNDKDLFKPIVHRLLHEGDPFFVLADLESYIAAHENVNKLFKEPDSWTKISIYNTAGMGFFSSDRAIQDYARDIWHVPTKSCSGEGN
|
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity).
|
Q9Z8N6
|
LPXD_CHLPN
|
UDP-3-O-acylglucosamine N-acyltransferase (EC 2.3.1.191)
|
MSEAPVYTLKQLAELLQVEVQGNIETPISGVEDISQAQPHHIAFLDNEKYSSFLKNTKAGAIILSRSQAMQHAHLKKNFLITNESPSLTFQKCIELFIEPVTSGFPGIHPTAVIHPTARIEKNVTIEPYVVISQHAHIGSDTYIGAGSVIGAHSVLGANCLIHPKVVIRERVLMGNRVVVQPGAVLGSCGFGYITNAFGHHKPLKHLGYVIVGDDVEIGANTTIDRGRFKNTVIHEGTKIDNQVQVAHHVEIGKHSIIVAQAGIAGSTKIGEHVIIGGQTGITGHISIADHVIMIAQTGVTKSITSPGIYGGAPARPYQETHRLIAKIRNLPKTEERLSKLEKQVRDLSTPSLAEIPSEI
|
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}.
|
Q9Z8N9
|
RECR_CHLPN
|
Recombination protein RecR
|
MTRYPDYLSKLIFFLRKLPGIGFKTAEKLAFELISWDSEQLKILGNAFHNVASERSHCPLCFTLKESKEADCHFCREERDNQSLCIVASPKDVFFLERSKVFKGRYHVLGSLLSPITGKHIENERLSILKSRIETLCPKEIILAIDATLEGDATALFLKQELQHFSVNISRLALGLPIGLSFDYVDSGTLARAFSGRHSY
|
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}.
|
Q9Z8P3
|
ACP_CHLPN
|
Acyl carrier protein (ACP)
|
MSLEDDVIAIIVEQLGVDPKEVNENSSFIEDLNADSLDLTELIMTLEEKFAFEISEEDAEKLRTVGDVFTYIKKRQAEQ
|
Carrier of the growing fatty acid chain in fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}.
|
Q9Z8R5
|
KTHY_CHLPN
|
Thymidylate kinase (EC 2.7.4.9) (dTMP kinase)
|
MFIVIEGGEGSGKSSLAKALGDQLVAQDRKVLLTREPGGCLIGERLRDLILEPPHLELSRCCELFLFLGSRAQHIQEVIIPALRDGYIVICERFHDSTIVYQGIAEGLGADFVADLCSKVVGPTPFLPNFVLLLDIPADIGLQRKHRQKVFDKFEKKPLSYHNRIREGFLSLASADPSRYLVLDARESLASLIDKVMLHTQLGLCT
|
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
|
Q9Z8S4
|
UBIX_CHLPN
|
Flavin prenyltransferase UbiX (EC 2.5.1.129)
|
MKRYVVGISGASGVILAVKLIKELVNAKHQVEVIISPSGRKTLYYELGCQSFDALFSEENLEYIHTHSIQAIESSLASGSCPVEATIIIPCSMTTVAAISIGLADNLLRRVADVALKERRPLILVPRETPLHTIHLENLLKLSKSGATIFPPMPMWYFKPQSVEDLENALVGKILAYLNIPSDLTKQWSNPE
|
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}.
|
Q9Z8S6
|
SURE_CHLPN
|
5'-nucleotidase SurE (EC 3.1.3.5) (Nucleoside 5'-monophosphate phosphohydrolase)
|
MVLMNKRLKIILTNDDGITAKGMSCLVSALLEANIGDIYIAAPQAEQSGKSMAISLNQVVCASPYAYPQPVKEAWAVGGSPTDCVRLGLRTLFESVSPDLVISGINCGNNICKNAWYSGTIGAAKQALVDGIPSMALSQDNHISFFQQDKAPEILKALVIYLLSQPFPCLTGLNINFPTSPGGSSWEGMRLVPPGDEFFYEEPQYLGSVNKNQYYVGKISGVRIGEHPSEELACMLENHISVSPIFSQNSPIGLMTLEEFQKTQENFNASLLSSELTTKIF
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. {ECO:0000255|HAMAP-Rule:MF_00060}.
|
Q9Z8T7
|
RL13_CHLPN
|
Large ribosomal subunit protein uL13 (50S ribosomal protein L13)
|
MEKRKDTKTTIVKSSETTKSWYVVDAAGKTLGRLSSEVAKILRGKHKVTYTPHVAMGDGVIVINAEKVRLTGAKKGQKIYRYYTGYISGMREIPFENMMARKPNYIIEHAIKGMMPRTRLGKKQLKSLRIVKGDSYETFESQKPILLDI
|
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}.
|
Q9Z8U7
|
YQGF_CHLPN
|
Putative pre-16S rRNA nuclease (EC 3.1.-.-)
|
MSKPSSCKAYLGIDYGKKRIGLAYAAEPLLLTLPIGNIEAGKNLKLSAEALHKIILSRNITCVVLGNPLPMQKGLYSSLQEEVSLLAEELKKLSTVEIILWDERLSSVQAERMLKQDCGLSRKDRKGKTDSLAATLILTSFLDSLPKKLTL
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00651}.
|
Q9Z8U9
|
KDSB_CHLPN
|
3-deoxy-manno-octulosonate cytidylyltransferase (EC 2.7.7.38) (CMP-2-keto-3-deoxyoctulosonic acid synthase) (CKS) (CMP-KDO synthase)
|
MKPEESECLCIGVLPARWNSSRYPGKPLAKIHGKSLIQRTYENASQSSLLDKIVVATDDQHIIDHVTDFGGYAVMTSPTCSNGTERTGEVARKYFPKAEIIVNIQGDEPCLNSEVVDALVQKLRSSPEAELVTPVALTTDREEILTEKKVKCVFDSEGRALYFSRSPIPFILKKATPVYLHIGVYAFKREALFRYLQHSSTPLSDAEDLEQLRFLEHGGKIHVCIVDAKSPSVDYPEDIAKVEQYITCLSNAYF
|
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.
|
Q9Z8V7
|
BDBC_CHLPN
|
Probable disulfide formation protein (Disulfide oxidoreductase) (Thiol-disulfide oxidoreductase)
|
MINFIRSYALYFAWAISCAGTLISIFYSYILNVEPCILCYYQRICLFPLTVILGISAYREDSSIKLYILPQAVLGLGISIYQVFLQEIPGMQLDICGRVSCSTKIFLFSYVTIPMASVVAFGAIVCLLVLTKKYRG
|
Required for disulfide bond formation in some proteins. {ECO:0000255|HAMAP-Rule:MF_00287}.
|
Q9Z8Z1
|
ARGR_CHLPN
|
Arginine repressor
|
MKKKVTIDEALKEILRLEGAATQEELCAKLLAQGFATTQSSVSRWLRKIQAVKVAGERGARYSLPSSTEKTTTRHLVLSIRHNASLIVIRTVPGSASWIAALLDQGLKDEILGTLAGDDTIFVTPIDEGRLPLLMVSIANLLQVFLD
|
Regulates arginine biosynthesis genes.
|
Q9Z900
|
EFP1_CHLPN
|
Elongation factor P 1 (EF-P 1)
|
MVLSSQLSVGMFISTKDGLYKVTSVSKVAGPKGESFIKVALQAADSDVVIERNFKATQEVKEAQFETRTLEYLYLEDESYLFLDLGNYEKLFIPQEIMKDNFLFLKAGVTVSAMVYDNVVFSVELPHFLELMVSKTDFPGDSLSLSGGVKKALLETGIEVMVPPFVEIGDVIKIDTRTCEYIQRV
|
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).
|
Q9Z901
|
BCCP_CHLPN
|
Biotin carboxyl carrier protein of acetyl-CoA carboxylase (BCCP)
|
MDLKQIEKLMIAMGRNGMKRFAIKREGLELELERDTREGNRQEPVFYDSRLFSGFSQERPIPTDPKKDTIKETTTENSETSTTTSSGDFISSPLVGTFYGSPAPDSPSFVKPGDIVSEDTIVCIVEAMKVMNEVKAGMSGRVLEVLITNGDPVQFGSKLFRIAKDAS
|
This protein is a component of the acetyl coenzyme A carboxylase complex first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
|
Q9Z963
|
RL19_CHLPN
|
Large ribosomal subunit protein bL19 (50S ribosomal protein L19)
|
MVNLLKELEQEQCRNDLPEFHVGDTIRLATKISEGGKERVQVFQGTVMARRGGGSGETVSLHRVAYGEGMEKSFLLNSPRIVSIEIVKRGKVARARLYYLRGKTGKAAKVKEFVGPRSSKK
|
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.
|
Q9Z964
|
TRMD_CHLPN
|
tRNA (guanine-N(1)-)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase)
|
MKIDILSLFPGYFDGPLQTSILGRAIKQRLLDVQLTNLRDFGLGKWKQVDDTPFSGGGMLLMAEPVTSAIRSVRKENSKVIYLSPQGALLTAEKSRELAAASHLILLCGHYEGIDERAIESEVDEEISIGDYVLTNGGIAALVLIDAVSRFIPGVLGNQESAERDSLENGLLEGPQYTRPREFEGKEVPEVLLQGDHKAISQWRLEQSERRTYERRPDLYLNYLYKRSIDHKFDEETTTNRDHFKCDKISVVLEVNKLKRAKNFYCKVFGLDAMSCENKFCLPHEGKTIFWLREVQAEKKNIVTLSLSLDCACEEDFCYLLRRWELFGGKLLEKQADEHAVWALAQDLDGHAWIFSWHRMK
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q9Z968
|
RF1_CHLPN
|
Peptide chain release factor 1 (RF-1)
|
MKKKVAEYLNRLAEVEIKISNPEIFSNSKEYSALSKEHSYLLELKNAYDKILNLEKVLADDKQALAIEKDPEMVVMLEEGINENKVELEKLNKILESLLVPPDPDDDLNVIMELRAGTGGEEAALFVGDCVRMYHLYASSKGWKYEVLSASESDLKGYKEYVMGISGTGVKRLLQYEAGTHRVQRVPETETQGRVHTSAITIAVLPEPSEEDTELLINEKDLKIDTFRASGAGGQHVNVTDSAVRITHLPTGVVVTCQDERSQHKNKDKAMRILKARIRDAEMQKRHNEASAMRSAQVGSGDRSERIRTYNFSQNRVTDHRIGLTLYNLDKVMEGDLDPITTAMVSHAYHQLLEHGN
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
Q9Z990
|
VATI_CHLPN
|
V-type ATP synthase subunit I (V-ATPase subunit I)
|
MRLNIHKYLFIGRNKADFFSASRELGVVEFISKKCFITTEQGHRFVECLKVFDHLEAEYSLEALEFVKDESVSVEDIVSEVLTLNKEIKGLLETVKALRKEIVRVKPLGAFSSSEIAELSRKTGISLRFFYRTHKDNEDLEEDSPNVFYLSTAYNFDYYLVLGVVDLPRDRYTEIEAPRSVNELQVDLANLQREIRNRSDRLCDLYAYRREVLRGLCNYDNEQRLHQAKECCEDLFDGKVFAVAGWVIVDRIKELQSLCNRYQIYMERVPVDPDETIPTYLENKGVGMMGEDLVQIYDTPAYSDKDPSTWVFFAFVLFFSMIVNDAGYGLLFLMSSLLFSWKFRRKMKFSKHLSRMLKMTAILGLGCICWGTTTTSFFGMSFSKTSVFREYSMTHVLALKKAEYYLQMRPKAYKELTNEYPSLKAIRDPKAFLLATEIGSAGIESRYVVYDKFIDNILMELALFIGVVHLSLGMLRYLRYRYSGIGWILFMVSAYLYVPIYLGTVSLIHYLFHVPYELGGQIGYYGMFGGIGLAVVLAMIQRSWRGVEEIISVIQVFSDVLSYLRIYALGLAGAMMGATFNQMGARLPMLLGSIVILLGHSVNIILSIMGGVIHGLRLNFIEWYHYSFDGGGRPLRPLRKIVCSEDAEASGIHLDNNSIV
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q9Z991
|
VATD_CHLPN
|
V-type ATP synthase subunit D (V-ATPase subunit D)
|
MSVQVKLTKNSFRLEKQKLARLQTYLPTLKLKKALLQAEVQNAVKDAAECDKDYVQAYERIYAFAELFSIPLCTDCVEKSFEIQSIDNDFENIAGVEVPIVREVTLFPASYSLLGTPIWLDTMLSASKELVVKKVMAEVSKERLKILEEELRAVSIRVNLFEKKLIPETTKILKKIAVFLSDRSITDVGQVKMAKKKIELRKARGDECV
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q9Z992
|
VATB_CHLPN
|
V-type ATP synthase beta chain (V-ATPase subunit B)
|
MQTIYTKITDIKGNLITVEAEGARLGELATITRSDGRSSYASVLRFDLKKVTLQVFGGTSGLSTGDHVTFLGRPMEVTFGSSLLGRRLNGIGKPIDNEGECFGEPIEIATPTFNPVCRIVPRSMVRTNIPMIDVFNCLVKSQKIPIFSSSGEHHNALLMRIAAQTDADIVVIGGMGLTFVDYSFFVEESKKLGFADKCVMFIHKAVDAPVECVLVPDMALACAEKFAVEEKKNVLVLLTDMTAFADALKEISITMDQIPANRGYPGSLYSDLALRYEKAVEIADGGSITLITVTTMPSDDITHPVPDNTGYITEGQFYLRNNRIDPFGSLSRLKQLVIGKVTREDHGDLANALIRLYADSRKATERMAMGFKLSNWDKKLLAFSELFETRLMSLEVNIPLEEALDIGWKILAQSFTSEEVGIKAQLINKYWPKACLSK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
|
Q9Z993
|
VATA_CHLPN
|
V-type ATP synthase alpha chain (EC 7.1.2.2) (V-ATPase subunit A)
|
MVTVSEQTAQGHVIEAYGNLLRVRFDGYVRQGEVAYVNVDNTWLKAEVIEVADQEVKVQVFEDTQGACRGALVTFSGHLLEAELGPGLLQGIFDGLQNRLEVLAEDSSFLQRGKHVNAISDHNLWNYTPVASVGDTLRRGDLLGTVPEGRFTHKIMVPFSCFQEVTLTWVISEGTYNAHTVVAKARDAQGKECAFTMVQRWPIKQAFIEGEKIPAHKIMDVGLRILDTQIPVLKGGTFCTPGPFGAGKTVLQHHLSKYAAVDIVILCACGERAGEVVEVLQEFPHLIDPHTGKSLMHRTCIICNTSSMPVAARESSIYLGVTIAEYYRQMGLDILLLADSTSRWAQALREISGRLEEIPGEEAFPAYLSSRIAAFYERGGAITTKDGSEGSLTICGAVSPAGGNFEEPVTQSTLAVVGAFCGLSKARADARRYPSIDPLISWSKYLNQVGQILEEKVSGWGGAVKKAAQFLEKGSEIGKRMEVVGEEGVSMEDMEIYLKAELYDFCYLQQNAFDPVDCYCPFERQIELFSLISRIFDAKFVFDSPDDARSFFLELQSKIKTLNGLKFLSEEYHESKEVIVRLLEKTMVQMA
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit (By similarity).
|
Q9Z995
|
VATE_CHLPN
|
V-type ATP synthase subunit E (V-ATPase subunit E)
|
MANLNADGKLKQICDALRLDTLKPAEDEAAALLHNAKEQAKRIIQEAQEEARKILETAEERAHQKIKQGEVALSQAGKRALEALKQAVENKIFRESLVEWLEHVTTDPEVSTKLIQALVQALEAQGVSGNLTAYIGKHVSPRAVNELLGKAVTTKLRKKSVVVGSFVGGVQLKVEEKNWVLDLSSSALLEIFTRYLQKDFREMIFQGS
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q9Z9A1
|
RL7_CHLPN
|
Large ribosomal subunit protein bL12 (50S ribosomal protein L7/L12)
|
MTTESLETLVEKLSNLTVLELSQLKKLLEEKWDVTASAPVVAVAAGGGGEAPVAAEPTEFAVTLEDVPADKKIGVLKVVREVTGLALKEAKEMTEGLPKTVKEKTSKSDAEDTVKKLQDAGAKASFKGL
|
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}.
|
Q9Z9A2
|
RL10_CHLPN
|
Large ribosomal subunit protein uL10 (50S ribosomal protein L10)
|
MKQEKTLLLQEVEDKISAAQGFILLRYLRFTAAYSREFRNSLSGVSAEFEVLKKRIFFKAIEAAGLEVDCSDTDGHLGVVFSCGDPVSAAKQVLDFNKQHKDSLVFLAGRMDNASLSGAEVEAVAKLPSLKELRQQVVGLFAAPMSQVVGIMNSVLSGVISCVDQKAGKN
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
Q9Z9A3
|
RL1_CHLPN
|
Large ribosomal subunit protein uL1 (50S ribosomal protein L1)
|
MTKHGKRIRGILKNYDFSKSYSLREAIDILKQCPPVRFDQTVDVSIKLGIDPKKSDQQIRGAVFLPNGTGKTLRILVFASGNKVKEAVEAGADFMGSDDLVEKIKSGWLEFDVAVATPDMMREVGKLGKVLGPRNLMPTPKTGTVTTDVAKAISELRKGKIEFKADRAGVCNVGVGKLSFESSQIKENIEALSSALIKAKPPAAKGQYLVSFTISSTMGPGISIDTRELMAS
|
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}.
|
Q9Z9A4
|
RL11_CHLPN
|
Large ribosomal subunit protein uL11 (50S ribosomal protein L11)
|
MSVKKVIKIIKLQIPGGKANPAPPIGPALGAAGVNIMGFCKEFNAATQDKPGDLLPVVITVYADKTFTFITKQPPVSSLIKKTLNLESGSKIPNRNKVGKLTQAQVEAIAEQKMKDMDIVLLESAKRMVEGTARSMGIDVE
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. {ECO:0000255|HAMAP-Rule:MF_00736}.
|
Q9Z9A5
|
NUSG_CHLPN
|
Transcription termination/antitermination protein NusG
|
MYKWYVVQVFTAQEKKVKKALEDFKESSGMTDFIQEIILPIENVMEVKKGEHKVVEKYIWPGYLLVKMHLTDESWLYVKSTAGIVEFLGGGVPVALSEDEVRSILTDIEEKKSGVVQKHQFEVGSRVKINDGVFVNFIGTVSEVFHDKGRLSVMVSIFGRETRVDDLEFWQVEEVAPGQESE
|
Participates in transcription elongation, termination and antitermination. {ECO:0000255|HAMAP-Rule:MF_00948}.
|
Q9Z9A8
|
IF1_CHLPN
|
Translation initiation factor IF-1
|
MAKKEDTLVLEGKVEELLPGMHFRVILENGMPVTAHLCGKMRMSNIRLLVGDRVTVEMSAYDLTKARVVYRHR
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. {ECO:0000255|HAMAP-Rule:MF_00075}.
|
Q9Z9C2
|
DUT_CHLPN
|
Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase)
|
MTVFCELDSGGELPEYTTPGAAGADLRANIEEPIALLPGQRALIPTGIKAEIPEGYELQVRPRSGLALKHGITVLNSPGTIDSDYRGEIRVILINFGDSTFIIEPKMRIAQVVLSPVVQATFVVKQESLAETARGSGGFGHTGAS
|
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}.
|
Q9Z9C9
|
HEM3_CHLPN
|
Probable porphobilinogen deaminase (PBG) (EC 2.5.1.61) (Hydroxymethylbilane synthase) (HMBS) (Pre-uroporphyrinogen synthase)
|
MLSVCYSDPCLSDFCQGKRPLRIASRNSNLAKAQVHECISLLRSWYPKLWFQLSTTETTGDREKKIPLHLVENSYFFTDGVDALVHKGVCDLAIHSAKDLPETPSLPVVAITRCLHPADLLVYADHYVHEPLPLSPRLGSSSLRRSAVLKQLFPQGQILDIRGTIEERLDQLHRGHYDAIVLAKAASLRLHLHHAYSIELPPPYHALQGSLAITAKDHAGKWKQLFTPIHCHSS
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Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
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Q9Z9E2
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Y039_CHLPN
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Nucleoid-associated protein CPn_0039/CP_0736/CPj0039/CpB0043
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MGSGYAKKKKEAKIMEQQFLEMEASLLEKRYEGQAGNGLVSVVINGKCDLISVKVQPTCLDPEDPEVIEDLFRAAFKLAKEQMDQEMSLMRSTMPF
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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}.
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Q9Z9E4
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PTHP_CHLPN
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Phosphocarrier protein HPr (Histidine-containing protein)
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MNEPTRTYLESEKDTQDQIEELQATCIVKNAAGIHVRPAGVIVRLFDGEPCDVHFTYAGKTINAKSIMSILMLGAPQGGEILVTIRSKEAHRILQKIQDAFSSGFGEL
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General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain.
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Q9Z9F7
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XERC_CHLPN
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Tyrosine recombinase XerC
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MIASIYSFLDYLKMVKSASPHTLRNYCLDLNGLKIFLEERGNLAPSSPLQLATEKRKVSELPFSLFTKEHVRMYIAKLIENGKAKRTIKRCLSSIKSFAHYCVIQKILLENPAETIHGPRLPKELPSPMTYAQVEVLMATPDISKYHGLRDRCLMELFYSSGLRISEIVAVNKQDFDLSTHLIRIRGKGKKERIIPVTSNAIQWIQIYLNHPDRKRLEKDPQAIFLNRFGRRISTRSIDRSFQEYLRRSGLSGHITPHTIRHTIATHWLESGMDLKTIQALLGHSSLETTTVYTQVSVKLKKQTHQEAHPHA
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Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. {ECO:0000255|HAMAP-Rule:MF_01808}.
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Q9Z9F9
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NTPP_CHLPN
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Nucleoside triphosphate pyrophosphatase (EC 3.6.1.9) (Nucleotide pyrophosphatase) (Nucleotide PPase)
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MSLPLVLGSSSPRRKFILEKFRVPFTVIPSNFDESKVSYSGDPIAYTQELAAQKAYAVSELHSPCDCIILTGDTIVSYDGRIFTKPQDKADAIQMLKTLRNQTHDVVTSIAVLHKGKLLTGSETSQISLTMIPDHRIESYIDTVGTLNNCGAYDVCHGGLILKKVHGCVYNVQGLPIQTLKYLLEELNIDLWDYSI
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Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. {ECO:0000255|HAMAP-Rule:MF_00528}.
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Q9Z9G6
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GATB_CHLPN
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Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT subunit B) (EC 6.3.5.-)
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MSAVYADWESVIGLEVHVELNTASKLFSSALNRFGDEPNTNISTVCTGLPGSLPVLNQSAVEKAVLFGCAVEGEISLLSRFDRKSYFYPDSPRNFQITQFEHPIIRGGRIKAIVQGEERYFELAQTHIEDDAGMLKHFGEFAGVDYNRAGVPLIEIVSKPCMFCPEDAVAYATSLVSLLDYIGISDCNMEEGSIRFDVNVSVRPKGSPELRNKVEIKNMNSFAFMAQALEAEKQRQIDEYLNQPNKDPKLVIPAATYRWDPEKKKTVLMRLKESAEDYKYFPEPDLPTLQLTESYIERIRKTLPELPYDKYHRYIQEYGLSEDIASILISDKNIATFFEVACKDCKNFRSLSNWVTVEFGGRCKTLGVKLPSSGIFPEGVAQLVNAIDQGVITGKIAKEIADLMMESPGKNPEEILKEKPELLPMSDEGELQKIIAEVVLANPESIVDYKNGKTKALGFLVGQIMKRTAGKAPPKRVNELLLLELDKG
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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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Q9Z9G7
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GATA_CHLPN
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Glutamyl-tRNA(Gln) amidotransferase subunit A (Glu-ADT subunit A) (EC 6.3.5.7)
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MYRYSALELAKAVTLGELTATGVTQHFFHRIEEAEGQVGAFISLCKEQALEQAELIDKKRSRGEPLGKLAGVPVGIKDNIHVTGLKTTCASRVLENYQPPFDATVVERIKKEDGIILGKLNMDEFAMGSTTLYSAFHPTHNPWDLSRVPGGSSGGSAAAVSARFCPVALGSDTGGSIRQPAAFCGVVGFKPSYGAVSRYGLVAFASSLDQIGPLANTVEDVALMMDVFSGRDPKDATSREFFRDSFMSKLSTEVPKVIGVPRTFLEGLRDDIRENFFSSLAIFEGEGTHLVDVELDILSHAVSIYYILASAEAATNLARFDGVRYGYRSPQAHTISQLYDLSRGEGFGKEVMRRILLGNYVLSAERQNVYYKKATAVRAKIVKAFRTAFEKCEILAMPVCSSPAFEIGEILDPVTLYLQDIYTVAMNLAYLPAIAVPSGFSKEGLPLGLQIIGQQGQDQQVCQVGYSFQEHAQIKQLFSKRYAKSVVLGGQS
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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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Q9Z9G8
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GATC_CHLPN
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Glutamyl-tRNA(Gln) amidotransferase subunit C (Glu-ADT subunit C) (EC 6.3.5.-)
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MEQFHLDREEILLLAKASALQLSEELIQEYQTSLSAVITSMKEALAIEIDDADSCESLFMHVVNVEDLREDSVTSDFNREEFLRNVPESLGGLVKVPAVIK
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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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Q9Z9J3
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ECFA1_HALH5
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Energy-coupling factor transporter ATP-binding protein EcfA1 (ECF transporter A component EcfA1) (EC 7.-.-.-)
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MEKGLLLESVSYQYDANAAPVLKEIDIHVPLGEWVAVIGPNGSGKSTLAKLLNGLLLPTSGRVTFNGMSTMDEGTHWEIRQQVGLVFQNPEHQFVATTVRDDLAFGMENRGFPREKMIQRIEEVSIQVGIDHLLDEEPHRLSGGQKQRVAIAGILAVEPSVIVFDEATSMLDPQGRKDVLETMKQLHENGMTIISITHDVNEASQAGRVLLLEKGEVMLDGSPAVVFHEQDKLEAAGIDRPFAYQLQLALQSRGIQLEGALLKKEELVEALWKYKSSN
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ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. {ECO:0000255|HAMAP-Rule:MF_01710}.
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