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   04-NOV-2026, entry version 156.
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};
GN   OrderedLocusNames=TM_0459;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
OC   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=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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; Evidence={ECO:0000255|HAMAP-
CC         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; Evidence={ECO:0000255|HAMAP-
CC         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; WP_004081507.1; NC_000853.1.
DR   AlphaFoldDB; P36252; -.
DR   SMR; P36252; -.
DR   FunCoup; P36252; 329.
DR   STRING; 243274.TM_0459; -.
DR   PaxDb; 243274-TM_0459; -.
DR   EnsemblBacteria; AAD35544; AAD35544; TM_0459.
DR   KEGG; tma:TM0459; -.
DR   KEGG; tmi:THEMA_02395; -.
DR   KEGG; tmw:THMA_0469; -.
DR   PATRIC; fig|243274.18.peg.471; -.
DR   eggNOG; COG0086; Bacteria.
DR   InParanoid; P36252; -.
DR   OMA; AACYGWD; -.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 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:DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd02655; RNAP_beta'_C; 1.
DR   CDD; cd01609; RNAP_beta'_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.1790.20; -; 1.
DR   Gene3D; 1.10.40.90; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 4.
DR   Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 2.
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; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 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
//