RPOC_DESVV
ID RPOC_DESVV Reviewed; 1385 AA.
AC A1VAJ5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Dvul_0438;
OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=391774;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP4;
RX PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA Stahl D.A.;
RT "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT plasticity.";
RL Environ. Microbiol. 11:2244-2252(2009).
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; CP000527; ABM27461.1; -; Genomic_DNA.
DR RefSeq; WP_010940189.1; NC_008751.1.
DR AlphaFoldDB; A1VAJ5; -.
DR SMR; A1VAJ5; -.
DR PRIDE; A1VAJ5; -.
DR EnsemblBacteria; ABM27461; ABM27461; Dvul_0438.
DR KEGG; dvl:Dvul_0438; -.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000009173; 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; 2.
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..1385
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308833"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 809
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 883
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 890
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"
SQ SEQUENCE 1385 AA; 154813 MW; 1B7C3027F1EF7907 CRC64;
MTLDDLFTVR GSAANIANIR NLKAIQITIA SPENIREWSY GEVKKPETIN YRTFKPERDG
LFCAKIFGPV KDYECNCGKY KRMKHRGIVC EKCGVEVIAS KVRRERMGHI ELAAPVAHIW
FLKTLPSKIG TLLDMTMADL EKVLYFDSYI VLDPGSTNLT KMQVISEDQY LQVIDHYGED
ALTVGMGAEA VRSLLEELNL EELRVQLREE SQATKSQTKK KKLTKRLKIV EAFLESNNKP
EWMVMEVIPV IPPELRPLVP LDGGRFATSD LNDLYRRVIN RNNRLKRLME LGAPDIIIRN
EKRMLQEAVD ALFDNGRRGR AITGTNGRPL KSLSDMIKGK QGRFRQNLLG KRVDYSGRSV
IVVGPKLKLH QCGLPKKMAL ELFKPFIYSE LEKRGLASTI KSAKKMVERE ELVVWDILEE
VVREYPIMLN RAPTLHRLGI QSFEPLLVEG KAIQLHPLVC SAYNADFDGD QMAVHVPLSV
EAQIECRVLM MSTNNILSPA NGSPVIVPSQ DIVLGLYYMT VDRSFEKGEN MSFCAPWEVV
AAYDAGVVAL HARINVRMED GKVVRTTVGR ILVWELLPHC VPFSMVNTTL TKKNIARLVS
TAYRDAGTKA TVILCDRLKD VGYEYATRAG VTIAVKDLTI PSTKKGLIET AQNEVDDIER
QYRDGIITRT EKYNKVVDVW TKATQDVSNE MIREISSDIV EDPRTGAKEA NSSFNSIYMM
STSGARGNQD QMRQLAGMRG LMAKPSGEII ETPITSSFRE GLSVLQYFTS THGARKGLAD
TALKTANSGY LTRRLVDVVQ DVIVSEHDCG TVDGIELTHI KEGGEIKIPL ADRALGRVLL
YPVYDPETRD LLFPENTLVD ENVAKVLVER EVSSVMIRSA LTCQSDRGIC TLCYGRDLAR
GHIVNIGETV GIIAAQSIGE PGTQLTMRTF HIGGTASREI ERSSFEAQHP GRVILSRVKA
VRNRDGQYMV MGKSGQLAIV DDQGREREKY TLPNGSRLLV TEGEEIRKGQ ILAEWDPFNE
PFVSEVDGVI RFSDIVEGKT FQEKMDEATR MTTQTIIEYR TTNFRPSISI CDEHGEVKMR
GNNIPATYSL PVGAIIMVKN GQDLQAGDII ARKPRETSKT KDIVGGLPRV AELFEVRKPK
DMAVVSEIAG IVTYAGETKG KRKLVVTPEI GEAKEYLVPK GKHITVTDGD FVEAGDLLTE
GHPELHDILR TRGEKYLARY LTDEIQEVYR FQGVAIDDKH IEVIVRQMLK KVTVLDPGGT
TFLVGEQVDK GEFRVENTRA MGEGRTPATA EPLVLGITQA SLTTSSFISA ASFQETTKVL
TEASLRGKMD YLRGLKENVI VGRLIPAGTG YREYVNTDIL VPEQRERPDK FLEDLEENPL
LVDIY
