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
