RPOC_MAGMM
ID RPOC_MAGMM Reviewed; 1412 AA.
AC A0L5W7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, 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=Mmc1_0841;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(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; CP000471; ABK43360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0L5W7; -.
DR SMR; A0L5W7; -.
DR STRING; 156889.Mmc1_0841; -.
DR PRIDE; A0L5W7; -.
DR EnsemblBacteria; ABK43360; ABK43360; Mmc1_0841.
DR KEGG; mgm:Mmc1_0841; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000002586; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1412
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308850"
FT REGION 1387..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
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 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 819
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 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 903
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1412 AA; 157052 MW; 5B71C18B54E890E2 CRC64;
MTPVSDAPAT PSSEISAAGQ SVFKLFSRPM LGQSFDGIRI SIASPEKIRS WSFGEVKKPE
TINYRTFKPE RDGLFCAKIF GPVKDYECLC GKYKRLKHRG VVCEKCGVEV IQSKVRRERM
GHIELAAPVA HIWFLKSLPS RIGLLLDMTL KDLERVLYFE NFVVLESGMT PMKRGELLTE
DRYYQLIEEF GDEFRAGIGA EAIREMLVDL KIPEEINQLR DELRDTSSEA RRKKIVKRLH
TLEAFQDSKN SPEWMILEVI PVIPPELRPL VPLDGGRFAT SDLNDLYRRV INRNNRLKRL
FELKAPDIII RNEKRMLQES VDALFDNGRR GRVITGTNKR PLKSLSEMLK GKQGRFRLNL
LGKRVDYSGR SVIVVGPELK LHECGLPKKM ALELFKPFIY NRLEERGLAT TIKAAKRMVE
KEKGEVWDIL EEVIREHPVM LNRAPTLHRL GIQAFEPKLV EGKAIQLHPL VCTAFNADFD
GDQMAVHVPL SIEAQIEARV LMMSTNNILS PANGKPIIVP TQDIILGLYY MTSERANVAG
EGMIFSNTME VKQAFDAGVA NLHASIQCRF RGKRVHTTVG RMLLADMLPE RIDFQAINKL
ITKKEVTKLI DHTYRMCGTK DTVIFTDRLM AMGFAFACRA GISFGKDDMV IPEAKRKLVD
AAQEKVKEIE KQYTDGLITE GEKYNKVVDI WSHCTERVAD EMMGTISTDT VLNKDGEMVE
QPSFNSIFMM ANSGARGSAA QMRQLAGMRG LMAKPSGEIM ETPITANFRE GLTVLQYFIS
THGARKGLAD TALKTANSGY LTRRLVDVAQ DCIVREEDCG TSIGITVAAL VEGNDVVETL
GDRLLGRTPV SDIKDPITDE LLVKAGTIMD EDIVEKIENS NVDSVLIRSP LTCETTRGVC
VTCYGRDLAR GTRVTVGEAV GVIAAQSIGE PGTQLTMRTF HIGGTASRQA EQSHQETTHG
GVLKFHDLIT VQDRAGRYVV LSRNSEVSLH EAVEHEGQVE AGRERERYRI PYGARISSAP
GSVVEKGTTF AEWDPFAMPI ITEVEGIVKF GDLVDGVSLR ENMDDTTGLI SKEVTEWKGQ
SSKKGDMRPR ITLKDVNSNE TLMMPNGSEC RYYLPVGAVI VVNEGDHVHG GDIIAKVLRQ
STKNRDITGG LPRVVELFEA RKPKEHSFIA ENEGMVTYGK DLKGKRRLVV TPDSGEPMEY
LLPKGKQLAV NEGDWVRKGE PLMEGSPVPQ DILKVLGLEE LCRFMVNEIQ EVYRLQGVRI
NDKHIEVIVR QMLQKVQITD PGDTMFVSGE QVEKDDYLLE NVKTDKRGGR VATCTPLLLG
ITKASLSTPS FISAASFQET TRVLTEAAIS GRVDTLNGLK ENVIVGRLIP AGTGNILSQL
KKMGSLTKGE KSTQGGEQHV AKVASSSEVT EG
