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RPOC_CAMJR
ID   RPOC_CAMJR              Reviewed;        1517 AA.
AC   Q5HVY8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=CJE0529;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01322};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR   EMBL; CP000025; AAW35116.1; -; Genomic_DNA.
DR   RefSeq; WP_002867604.1; NC_003912.7.
DR   AlphaFoldDB; Q5HVY8; -.
DR   SMR; Q5HVY8; -.
DR   PRIDE; Q5HVY8; -.
DR   KEGG; cjr:CJE0529; -.
DR   HOGENOM; CLU_000524_3_1_7; -.
DR   OMA; YRNIRVE; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   SMART; SM00663; RPOLA_N; 1.
DR   TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..1517
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000225521"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         482
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         484
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         486
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         812
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         886
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         893
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         896
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1517 AA;  168837 MW;  640943FBD5C2100E CRC64;
     MSKFKVIEIK EDARPRDFEA FQLRLASPEK IKSWSYGEVK KPETINYRTL KPERDGLFCA
     KIFGPIRDYE CLCGKYKKMR FKGVKCEKCG VEVANSKVRR SRMGHIELVT PVAHIWYVNS
     LPSRIGTLLG VKMKDLERVL YYEAYIVENP GDAFYDNEST KKVEYCDVLN EEQYQNLMQR
     YENSGFKARM GGEVVRDLLA NLDLVALLNQ LKEEMGATNS EAKKKTIIKR LKVVENFLNS
     NLNANTDSDE AVPNRPEWMM ITNLPVLPPD LRPLVALDGG KFAVSDVNDL YRRVINRNTR
     LKKLMELDAP EIIIRNEKRM LQEAVDALFD NGRRANAVKG ANKRPLKSLS EIIKGKQGRF
     RQNLLGKRVD FSGRSVIVVG PKLRMDQCGL PKKMALELFK PHLLAKLEEK GYATTVKQAK
     KMIENKTNEV WECLEEVVKG HPVMLNRAPT LHKLSIQAFH PVLVEGKAIQ LHPLVCAAFN
     ADFDGDQMAV HVPLSQEAIA ECKVLMLSSM NILLPASGKS VTVPSQDMVL GIYYLSLEKA
     GAKGSHKICT GIDEVMMALE SKCLDIHASI QTMVDGRKIT TTAGRLIIKS ILPDFVPENS
     WNKVLKKKDI AALVDYVYKQ GGLEITASFL DRLKNLGFEY ATKAGISISI ADIIVPNDKQ
     KAIDEAKKQV REIQNSYNLG LITSGERYNK IIDIWKSTNN VLSKEMMKLV EKDKEGFNSI
     YMMADSGARG SAAQISQLAA MRGLMTKPDG SIIETPIISN FREGLNVLEY FISTHGARKG
     LADTALKTAN AGYLTRKLID VAQNVKITIE DCGTHEGVEI NEITADSSII ETLEERILGR
     VLAEDVIDPI TNSVLFAEGT LMDEEKAKIL GESGIKSVNI RTPITCKAKK GICAKCYGIN
     LGEGKLVKPG EAVGIISAQS IGEPGTQLTL RTFHSGGTAS TDLQDRQVSA QKEGFIRFYN
     LKTYKNKEGK NIVANRRNAA VLLVEPKIKT PFKGVINIEN IHEDVIVSIK DKKQEVKYIL
     RKYDLAKPNE LAGVSGSIDG KLYLPYQSGM QVEENESIVE VIKEGWNVPN RIPFASEILV
     EDGEPVVQNI KAGEKGTLKF YILKGDGLDR VKNVKKGDIV KEKGFFVVIA DENDREAKRH
     YIPRESKIEF NDSEKIDDAN TIIASAPKKE RKVIAEWDAY NNTIIAEIDG VVSFEDIEAG
     YSADEQIDEA TGKRSLVINE YLPSGVRPTL VIAGKGDKAV RYHLEPKTVI FVHDGDKIAQ
     ADILAKTPKA AAKSKDITGG LPRVSELFEA RKPKNAAVIA EIDGVVRFDK PLRSKERIII
     QAEDGTSAEY LIDKSKHIQV RDGEFIHAGE KLTDGVVSSH DVLKILGEKA LHYYLISEIQ
     QVYRGQGVVI SDKHIEVIVS QMLRQVKVVD SGHTKFIEGD LVSRRKFREE NERIIRMGGE
     PAIAEPVLLG VTRAAIGSDS VISAASFQET TKVLTEASIA GKFDYLEDLK ENVILGRMIP
     VGTGLYGEQN LKLKEQE
 
 
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