RPOC_CAUSK
ID RPOC_CAUSK Reviewed; 1394 AA.
AC B0SUP8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Caul_0795;
OS Caulobacter sp. (strain K31).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX NCBI_TaxID=366602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) 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; CP000927; ABZ69926.1; -; Genomic_DNA.
DR RefSeq; WP_012284865.1; NC_010338.1.
DR AlphaFoldDB; B0SUP8; -.
DR SMR; B0SUP8; -.
DR STRING; 366602.Caul_0795; -.
DR EnsemblBacteria; ABZ69926; ABZ69926; Caul_0795.
DR KEGG; cak:Caul_0795; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
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..1394
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353320"
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 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 810
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1394 AA; 154040 MW; 5E74C81B1B9A61F2 CRC64;
MNQEVLNIFN PVQAAPTFDQ IRISLASPEK IRSWSFGEIK KPETINYRTF KPERDGLFCA
RIFGPTKDYE CLCGKYKRMK YKGIICEKCG VEVTLARVRR ERMGHIELAS PVAHIWFLKS
LPSRIAMMLD MPLKDIERVL YFEYYIVTEP GLTPLKQHQL LSEDDFMRAQ DEYGDDSFTA
EIGAEAIQNL LKAIDLDKEA ERLREELAGT VSDMKQKKFS KRLKILEAFS ESGNRPEWMV
LTVVPVIPPE LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLIELRAP DIIIRNEKRM
LQESVDALFD NGRRGRVITG ANKRPLKSLA DMLKGKQGRF RQNLLGKRVD YSGRSVIVVG
PDLKLHECGL PKKMALELFK PFIYARLDAK GLSGTVKQSK RMVEREQPQV WDILEEVIRE
HPVMLNRAPT LHRLGIQAFE PKLIEGKAIQ LHPLVCAAFN ADFDGDQMAV HVPLSLEAQL
EARVLMMSTN NILSPANGRP IIVPSQDIVL GLYYLSVARE GEPGEGKIFA DLGEIEAAMD
AGVVSLHAKI KSRFTEMDAD GVVRRRVIDT TPGRMKIAAL LPQHTAIGHR LIEKALTKKE
IGNLIDVVYR HCGQKATVIF ADQIMGLGFK EAAKAGISFG KDDIIIPKRK EAIVAETRTL
AEEYEQQYAD GLITKGEKYN KVVDAWAKAT DRVADEMMAE LQMKHKDENG REKEINAIYM
MAHSGARGSQ AQMKQLGGMR GLMAKPSGEI IETPIVSNFK EGLTVQEYFN STHGARKGLA
DTALKTANSG YLTRRLVDVA QDCIIVEEDC GTTRGITLRA VVEGGDVLVS LGARVLGRFS
AEDIKDPATG EIVVPADTYL TENMADLIEA AAVQSVKVRS VLTCEAKIGV CGACYGRDLA
RGTPVNIGEA VGVIAAQSIG EPGTQLTMRT FHIGGTAQVA EQSFFESSND GTVRVTGATV
VGTDGFLVVM SRNTAVSVLV DGKERENYKP PYGARLKIKD GDKVKRGQRL ADWDPYTTPI
ITEVAGKIRA EDLVDGFSVR EETDEATGIA QRVIADWRTS ARASDLRPAM GVLAEDGSYV
RLANGGEARY LMSVGAILSV GDGDMVKPGE VIARIPTEGA KTRDITGGLP RVAELFEARR
PKDCAVIAEM DGRVEFGKDY KNKRRIKITP EVDADGNQGE PVEFLIPKGK HIAVHDGDFI
ARGEYIIDGN PDPHDILRIL GVEALANFLV DEIQEVYRLQ GVPINDKHIE TIVRQMLQKV
EILEPGDTGL IKGDHLDKPE FYVEQDRAVA RGGRPATTQP VLLGITKASL QTKSFISAAS
FQETTRVLTE ASVHGKTDTL EGLKENVIVG RLIPAGTGSY LRSLQRVAAK RDEQLAQQRE
DAMEPLPAVI AEEA
