RPOC_DESOH
ID RPOC_DESOH Reviewed; 1447 AA.
AC A8ZV52;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Dole_0703;
OS Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3;
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., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-2007) 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; CP000859; ABW66513.1; -; Genomic_DNA.
DR RefSeq; WP_012174132.1; NC_009943.1.
DR AlphaFoldDB; A8ZV52; -.
DR SMR; A8ZV52; -.
DR STRING; 96561.Dole_0703; -.
DR PRIDE; A8ZV52; -.
DR EnsemblBacteria; ABW66513; ABW66513; Dole_0703.
DR KEGG; dol:Dole_0703; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008561; 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:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
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; 3.10.50.40; -; 1.
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; IPR046357; PPIase_dom_sf.
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..1447
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141768"
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 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 964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 971
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 974
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1447 AA; 160381 MW; 74DDEC6B207C4ED6 CRC64;
METVYDFFAK PINPRRFSGV KIALASSEQI LQWSFGEITK PETINYRTFR PERDGLFCAK
IFGPTKDFEC NCGKYKRMKH RGVTCEKCGV EVIQSKVRRE RMAHIKLASP VSHIWFLKSL
PSKIGNVLDL TLKELERVLY FDSYIVIDPK NTDLSPMQLL SEEAYQEARA KYGSDFEAAI
GAEAIKALLD KVDLEVLSTQ LREDLKATSV EAKRKKLAKR LRIVDAFAKS GVSPSWMIIE
VVPVLPPDLR PLVPLEGGRF ATSDLNDLYR RVINRNNRLK RLMELKAPDI IIRNEKRMLQ
EAVDVLFDNG RHGRAVTGSN KRPLKSLTDT LKGKQGRFRQ NLLGKRVDYS GRTVITIGPN
LRLHQCGLPK QMALELFKPF IYYRLEQKGY VSTVKSAKKM VEREVPEVWD TLEEVVKEYP
VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHI PLSVEAQIEA
RVLMLATNNI LSPANGSPII VPTQDIVLGT YYMTKTIEGT KGEGVVFSGP EEVVAAFDSG
TVGLHAAISV RINGKLYDTS VGRVLVWEVI PQQIVPVFKT IHFSAKKEAN SVLAEIKRGA
SFVDMQKKHG DESGVDYERA MKKEDMITEF GLSEADADYL FSLKEGECSD IIGISDGYRL
FKLAGYRSEI PFEMVNRPLG KKAIRELVDG AYRNTGLKST VILADRLKDI GYKYSTLGGL
SISIDAMVVP EKKWDIIKAA EKKVEEIANQ YKEGLITQGE KYNKVVDIWS KATDDIANEM
MEAMRTDAGT PTGRFNPVFM MADSGARGSK DQMRQLAGMR GLMAKPSGEI IETPIVANFR
EGLSVLQYFI STHGARKGLA DTALKTANSG YLTRRLADVA QDCIITEDDC GAMMGVEVEA
LVEGGEIIER LVDRVIGRIA LEDIRDPFTD EVIVRGGEEI SERHLSVIEN SGLTKIWIRS
VLTCKSETGI CAKCYGRDFA HGKLVEHGQA VGILAAQSIG EPGTQLTMRT FHIGGTASRK
VERAEIRARV DGFVRLGDLK LVENAEKKLV VMNRRGGEFT IVNKAGREVE KCPVIYGATI
VVKDGQDIQA GDVLAAWDPF TTPIVAEVAG TVKFGDIVKG KTMQEMVDPV TGKSSQTIID
ESRTHDVRPR ISIKDDENKT ATLPDGKSKA RYPLPVGAVL LVEENDTIRA GDVIAKLPRA
TTKTKDITGG LPRVAELFEV RKPKEAAILS EINGYISIAK ATTKKGKQKV TVAPVDGGEP
REYLIPRGKH INVYDGDYIR AGEEIVAGSA NPQDVMNIRG DVALARYLVD EVQEVYRLQG
VTINDKHIEV IVRQMMRRVK IKEIGDTEFI DDEQVDRQRF EDTNREVIAN GGKPAVGEPL
ILGITKASLA TESFISAASF QETTKVLTDA SIAGKTDYLR GLKENVIMGR LIPAGTGFVE
YRKAAEK
