RPOC_THEMA
ID RPOC_THEMA Reviewed; 1690 AA.
AC P36252;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=TM_0459;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=8177738; DOI=10.1093/nar/21.21.4904;
RA Palm P., Schleper C., Arnold-Ammer I., Holz I., Meier T., Lottspeich F.,
RA Zillig W.;
RT "The DNA-dependent RNA-polymerase of Thermotoga maritima; characterisation
RT of the enzyme and the DNA-sequence of the genes for the large subunits.";
RL Nucleic Acids Res. 21:4904-4908(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X72695; CAA51247.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35544.1; -; Genomic_DNA.
DR PIR; S41467; S41467.
DR RefSeq; NP_228269.1; NC_000853.1.
DR RefSeq; WP_004081507.1; NZ_CP011107.1.
DR AlphaFoldDB; P36252; -.
DR SMR; P36252; -.
DR STRING; 243274.THEMA_02395; -.
DR EnsemblBacteria; AAD35544; AAD35544; TM_0459.
DR KEGG; tma:TM0459; -.
DR KEGG; tmw:THMA_0469; -.
DR PATRIC; fig|243274.18.peg.471; -.
DR eggNOG; COG0086; Bacteria.
DR InParanoid; P36252; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008183; 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; 2.
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.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1690
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067818"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 755
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 757
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1690 AA; 190521 MW; 9ED23FD2E9512CE6 CRC64;
MPMSSFKRKI KAIQIKIASP EVIRSWSGGE VKKPETINYR TFKPERDGLF CERIFGPVKD
YECACGKYKG KKYEGTVCER CGVRVESREA RRKRMGHIEL AAPAVHIWYL ESIPSVLGTL
LNMSTSDLEN IIYYGSRRVI ERAFIVTDPK DTPFSQGDVI YETEYRIYRK KWDFDVEQAF
VVKNPKSPVL SDIDGEVTLK TEKSITGREI TWIIVKNITR ATHTVLPGMI LVVKDGQEVE
KGQDLTKEMT IDPVYAPFDG HVEIDELSNT ITLKPLTTSK DQPVVFTIPY GAKILVSNGQ
KVKKGDQITT STSLPAVKAS ISGTVRFGSN LNIRALEDGN FEVLSTGEVY VEQVIEERKY
PVFEGALVYV NNGDQVKKGD HLADRFLFEE EYLSATEYKI FESHYPTMFD VEERTENDRP
IVVITDIDPE VSKETGLKVG DIVTENEYEA YLQIYPEKIV ADAGAQAIKK LLQNLDLEAL
QAEIEAELKK LPSSSSKAIK LRRRLKMVKD FLKSGNKPEW MVLEVVPVIP PDLRPMIQIE
GGRFATTDLN ELYRRLINRN NRLKKLLELG APEIILRNEK RMLQEAVDAL IHNGSDSEGK
RSRRAVLKDR NGRPLKSLTD LLKGKKGRFR RNLLGKRVDY SGRAVIVVGP NLKIHQCGIP
KKMAMELFKP FVLAKLLGEG SSSKTMRKVK KAIIEKEMPE AWEVLEEVIK GSVVLLNRAP
TLHRMSIQAF EPKLVEGNAI QLHPVVCPPF NADFDGDQMA VHVPLSAAAQ AEARFLMLSR
YNIISPAHGK PISLPTQDII IGSYYLTTVG KEFDSLKEED VKWKFSSPEE AMLAYHLGFI
KLHTPILIKV AVNGEEKRIK TTLGRVIFNG ILPEDLRDYN RIFDKKQINA LVYETFKRHG
IDRAADLLDD IKDIGFHYAT VSGLTLSLKD LKIPPERDEI LRKTWEKVRI IEENYEKGFL
TEEQRKSEII RLWMSVTEEI TKLTSKTLAE DPFNPIYMMV NSGARGNIDQ VKQLAGIRGL
MIKAYDPRSR EIKSKIFKGQ AIHEALTFDY PVDKNLREGV DILQFFISTY GARKGQVDTA
MNTSFAGYLT RRLVDVAQSV TVAEPDCGTH EGIRAMDLIK EGTVVEKMNE FLFGRVLARD
VLDPETKEVL KNPETGKEYT RNTMLTDDDA NFLASYKKMV DVVRYEEIDI TELSLPNMYA
EIAEPVGEYE EGTELTWDVI KAAKNEGKYR IKVKVYPVVG TVYAEEEPLY DKKGERQLLV
YQEVINEIVA KMLEENGIEK VSVRPDIIVR SPLTCESEYG VCAACYGMDL SNHKIVNVGE
AVGVVAAQSI GEPGTQLTMR TFHVGGVMGA SDIVSGLTTV EKTFEPYAFL REEKSGGKKE
IRKYYGSEAI LCEVDGFVKD IATDESGRTV IYIEDYAGNI HAYKVPKRAK VRVEKGQKVL
RGETLTSGAI VWWKLLELES EKGVMTAMNL LKIIKNAYVQ QGVSIHDKHF EIIFKQMLSM
ATIVDPGDSD YLPDQLVPLV DIKRFNREIL EGNAKVEENR KWVIGKTLAK RIITETEEGE
LVELAQKGDE VTEELLKKII EAGIKEIDVF EKDKVVTYQI LPKEPIKYKR RLLSLKKAAL
NYPGWLSAAA FEETAWVLTA AAIEGKVDPL IGLKENVIVG QLIPAGTGLD VFAGIQVEET
PRAAVEEELA
