RPOC_CAMLR
ID RPOC_CAMLR Reviewed; 1517 AA.
AC B9KFG8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Cla_0450;
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
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; CP000932; ACM63803.1; -; Genomic_DNA.
DR RefSeq; WP_012661186.1; NC_012039.1.
DR AlphaFoldDB; B9KFG8; -.
DR SMR; B9KFG8; -.
DR STRING; 306263.Cla_0450; -.
DR PRIDE; B9KFG8; -.
DR EnsemblBacteria; ACM63803; ACM63803; CLA_0450.
DR GeneID; 7411187; -.
DR KEGG; cla:CLA_0450; -.
DR PATRIC; fig|306263.5.peg.447; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000007727; Chromosome.
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; -; 2.
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_1000165837"
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; 168831 MW; 8BC6FD6E6E5E0B7F CRC64;
MSKFKPIEIK EDGRPRDFEA FQLRLASPEK IKSWSYGEVK KPETINYRTL KPERDGLFCA
KIFGPVRDYE CLCGKYKKMR FKGIKCEKCG VEVTTSKVRR SRMGHIELVT PVAHIWYVNS
LPSRIGTLLG VKMKDLERVL YYEAYIVENP GDAYYDNENS KKVEFCDVLN EEQYLNLMQR
YESSGFKARM GGEVVRDLLA NLDLVALLNQ LKEDIASTNS EAKKKTIIKR LKVVENFLNS
NLNSNTNIDE VVPNRPEWMM ITNLPVLPPD LRPLVALDGG KFAVSDVNDL YRRVINRNTR
LKRLMELDAP EIIIRNEKRM LQEAVDALFD NGRRANAVKG ANKRPLKSLS EIIKGKQGRF
RQNLLGKRVD FSGRSVIVVG PKLRMDQCGL PKKMALELFK PHLLAKLEEK GYATTVKQAK
KMIENKTNEV WECLEEVVKG HPVMLNRAPT LHKLSIQAFH PVLVEGKAIQ LHPLVCAAFN
ADFDGDQMAV HVPLSQEAIA ECKVLMLSSM NILLPASGRS VTVPSQDMVL GIYYLSLEKD
GAKGEHKICT GIEEVMIALE AKSLDIHASI RSVVDGRKIT TTAGRLIIKS ILPDFVPENM
WNKVMKKKDI AALVDYVYKE GGLEVSASFL DKLKDLGFEY ATKAGISISI ADIIVPDQKQ
KNIDEAKKQV REIQNSYNLG LITSGERYNK IIDIWKSTNN ILSKDMMELI KKDKEGFNSI
YMMADSGARG SAAQISQLAA MRGLMAKPDG SIIETPIISN FREGLNVLEY FISTHGARKG
LADTALKTAN AGYLTRKLID VAQNVKVTVD DCGAHEGVEI NEITADGVVI ETLEERILGR
VLAENIIDSI TNEILFSEGT LIDEEKARVI VESGVKSVSI RTPITCKAKK GVCSKCYGIN
LGEGKLVKPG EAVGIISAQS IGEPGTQLTL RTFHSGGTAS TDLQDRQVVA HKEGFVRFYN
LNTYEDRQGK TIVANHRNAA ILLVEPKIKA PFKGTIHIEH AYEDVVVSVK AKNNEAKFIL
RKYDLAKANE LAGVSGNIEG KLYIPYSDGV EVAENESIVE VIKEGWNIPN RIPYASELLV
KDGDPITQDI IAGAKGTLKF YMLKGDGLDR IKNLKKGDVV KEKGVFVVIA DENDREAKRH
YIPRESVIEF DDSAFVDNPK AIIAKSSKED KTIIAEWDAY NNTVIAEVAG TINFEDIESG
YSADEQIDEA TGKRSLVINE YLPSGVRPAI LILGEKGKMV RYQLEPKTVI YVNDGDKVKQ
ADILAKTPKA ATKSKDITGG LPRVSELFEA RKPKNTAVIA EIDGVVRFDK PLRSKERIII
QAEDGSSAEY LIDKSKRIQV RDGEFIHAGE KLTDGVISSH DVLRILGEKA LHYYLISEIQ
QVYRGQGVVI SDKHIEIIVS QMLRQVKIVD SGHTNFIVGD LVSRRKFREE NERILKYGGE
PAVAEPVLLG VTRAAIGSDS VISAASFQET TKVLTEASIA GKFDYLEDLK ENVILGRMIP
VGTGLYSEQN IKLKQQN
