RPOC_CAMFF
ID RPOC_CAMFF Reviewed; 1508 AA.
AC A0RQI4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
GN OrderedLocusNames=CFF8240_1314;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000487; ABK82615.1; -; Genomic_DNA.
DR RefSeq; WP_011732162.1; NC_008599.1.
DR AlphaFoldDB; A0RQI4; -.
DR SMR; A0RQI4; -.
DR STRING; 360106.CFF8240_1314; -.
DR EnsemblBacteria; ABK82615; ABK82615; CFF8240_1314.
DR GeneID; 61065133; -.
DR KEGG; cff:CFF8240_1314; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000760; 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..1508
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308824"
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 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1508 AA; 168011 MW; 317A65B07B38FF03 CRC64;
MSELKPIEIK EDAKPRDFEA FQLRLASPDR IKAWSHGEVK KPETINYRTL KPERDGLFCA
KIFGPIRDYE CLCGKYKKMR YKGIKCEKCG VEVTTSKVRR SRMGHIELVT PVAHIWYVNS
LPSRIGTLLG IKMKDLERVL YYEAYIVENP GDAFYDNENS KKVDLYDVLN EEQYVLLEQK
FSESGFKARM GGEVIRDLLA SLDLVSILDQ LKIEIESTNS EAKKKTIVKR LKVVESFLNS
GNRPEWMMIT NLPVLPPDLR PLVSLDGGKF AVSDVNDLYR RVINRNTRLK RLMELDAPEI
IIRNEKRMLQ EAVDALFDNG RRANAVKGAN KRPLKSLSEI IKGKQGRFRQ NLLGKRVDFS
GRSVIVVGPK LRMDQCGLPK KMALELFKPH LLARLEEKGY ATTVKQAKKM IEDKTNEVWE
CLEEVVADHP VMLNRAPTLH KMSIQAFHPV LIEGKAIQLH PLVCSAFNAD FDGDQMAVHV
PLSQEAIAEC KILMLSSMNI LLPASGKAVT VPSQDMVLGI YYLSLEKNEA VGANKIFASV
DEVMIAVEAH YLDLHAKIKT MVEGRTVFTT AGRLIIKSIL PNLKENSVPE SMWNKVMKKK
DIANLVDYVY KNGGLEVTAG FLDKLKNLGF RYATKAGISI SIADIIIPES KYSYVDEAKK
RVREIQNQYG SGLLTDSERY NKIVDIWTDT NNKVAAEMMK LIKTDKSGFN SIYMMADSGA
RGSAAQIRQL AGMRGLMAKP DGSIIETPIT SNFREGLNVL EYFISTHGAR KGLADTALKT
ANAGYLTRKL IDVAQNVKVT MDDCGTHEGV EITEITENGE LIESLEERVL GRVLSDDVID
PITNEILFTE GTLIDEVKAR TITDAGIKSV SIRTPITCKA SKGVCSKCYG INLGEGKLVK
PGEAVGIISA QSIGEPGTQL TLRTFHIGGT ASTEQQDRQV VAQKEGFIRY YNLKTYENNN
KFIVTNRRNA AILLVEPKIK APFDGEINIE VAHEDINVII KGKSDEVKYV LRKHDLAKPN
ELAGVSGKVE GKFYIPYIKG DKVKENESIV EVIKEGWNVP NRIPFASEVK VADGDPVTQD
ILSGANGVLK FYILKGDYLE RIKNVKKGDM VSEKGLFVVI ADDDDREAVR HYIPRNSVIK
FNDSDIVSAK DTIAKPQDGS KLVIAEWDPY STPVIAEEAG TVAYEDIEPG YSVAEQYDEA
TGESRLVINE YLPSGVKPTI VISTKSGKLI RYQLEPKTAI FVKDGAEVSR ADTIAKTPKA
VAKSKDITGG LPRVSELFEA RRPKNTAIIA EIDGTIKFDK PLRSKERIII MAEDGSSAEY
LIDKSRQIQV RDGEFVHAGE KLTDGLVSSH DVLRILGEKA LHYYLISEIQ QVYRSQGVAI
SDKHIEIIVS QMLRQVKIVD SGHTNFIVGD MVSRRKFREE NDRIMKIGGE PAIAEPVLLG
VTRAAIGSDS VISAASFQET TKVLTEASIA AKFDYLEDLK ENVILGRMIP VGTGLYQDKK
VKIKINED
