RPOC_SYNFM
ID RPOC_SYNFM Reviewed; 1351 AA.
AC A0LII5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Sfum_1550;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-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; CP000478; ABK17237.1; -; Genomic_DNA.
DR RefSeq; WP_011698408.1; NC_008554.1.
DR AlphaFoldDB; A0LII5; -.
DR SMR; A0LII5; -.
DR STRING; 335543.Sfum_1550; -.
DR PRIDE; A0LII5; -.
DR EnsemblBacteria; ABK17237; ABK17237; Sfum_1550.
DR KEGG; sfu:Sfum_1550; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001784; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1351
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308894"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 801
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 875
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 882
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"
SQ SEQUENCE 1351 AA; 150843 MW; B76BA00A191E98DE CRC64;
MKELYSLFMK PKDPLHFNAV KIMISSPERI REWSYGEVKK PETINYRTFK PERDGLFCAR
IFGPIKDYEC NCGKYKRMKH RGVVCEKCGV EVIQSKVRRE RMGHIELASP VAHIWFLRSL
PSKIGNLLDL TLRELEKVLY FDSYIVLDPG DTPLTKGELL TEEKYRQMVQ EHGSGFVAGI
GAESIKQLLA GLDLEKLAVE LREEMSKTNS MAKRKKLAKR LKIIDAFRES ENRPEWMIMD
VIPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLQELNAPDI IIRNEKRMLQ
EAVDVLFDNG RRGKTITGAS KRPLKSLSDM LKGKQGRFRQ NLLGKRVDYS GRTVIVIGPN
LRLHQCGLPK KMALELFKPF IYNKLEEKGY VTTIKAAKKM VERETPEVWD TLDEVVREFP
VMLNRAPTLH RLGIQAFEPI LIEGKAIQLH PLVCTAFNAD FDGDQMAVHV PLSIEAQAEA
RILMMSTNNI LSPAHGDPII VPSQDIVLGI YYMTREKPFA KGEDRVFSSR EEVRCAFDAG
EADLHARVHV RMGDERVKTT VGRVLLSEIL PEEMPFSAVN RVMNKKVLAG LIDMCYRTAG
IKATVLLADR LKDLGYEYAT RSGLSISIKD MTIPHRKSEI LDQAFDLVKE IERQYNEGLI
TEGEKYNKAV DIWAKATEDV AAEMMKEIAT TEVGGPEGEA RVVEAFNPIF MMADSGARGS
KDQMRQLAGM RGLMAKPSGE IIETPITANF REGLTVLQYF ISTHGARKGL ADTALKTANS
GYLTRRLVDV SQDVIISEPD CGTMDGIEVE ALLEAGEIIQ RLGDRILGRI AQEDILDPVT
AEVLVPMGTE IDEQRVQLIE DAGIEKVNIR SALTCRSLRG VCTMCYGRDL AQGKLAQIGE
AIGIIAAQSI GEPGTQLTMR TFHIGGTASK SIERTSINNR YAGTVRFLNL NTVHNRDGDL
IAMNRNGEIS IISESGRERE RYVIIYGAKL KVTDGQPVEP DTLLAEWDPF TTPILTEVAG
AAKFGDIVEG QTMQEKLDPV TGKSSKVVVE YRESDVRPRI SIKDDKGKTA RVGEGGFARY
FMPVGAILMV NEGDAIFPGD VLARIPRETT KTKDITGGLP RVAELFEVRK PKEHAVITEI
DGVIGFGKDT KGKRKVIVSP EVGDARDYLI PKGKHISVHE GDYVRAGEPL MDGSPNPHDI
LTVLGEKEVA KYLVDEVQQV YRLQGVKIND KHIEVIVRQM LKRVRITDPG DSEFLMGEHV
EKPIFEEINS KLTEEDKRPA AAEPLLLGIT KASLSTQSFI SAASFQETTK VLTDAATAGK
VDYLLGLKEN VIMGRLIPAG SGLRTYREVR K
