RPOC_THEAB
ID RPOC_THEAB Reviewed; 1649 AA.
AC B7ICR2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=THA_1344;
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=484019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B;
RX PubMed=19124572; DOI=10.1128/jb.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(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; CP001185; ACJ75789.1; -; Genomic_DNA.
DR AlphaFoldDB; B7ICR2; -.
DR SMR; B7ICR2; -.
DR STRING; 484019.THA_1344; -.
DR PRIDE; B7ICR2; -.
DR EnsemblBacteria; ACJ75789; ACJ75789; THA_1344.
DR KEGG; taf:THA_1344; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000002453; 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; 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.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1649
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000165856"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1077
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1649 AA; 184820 MW; 58C81D5E75CE8C39 CRC64;
MGSTFKREIA KVTVKVASPE VIRSWSSGEV KKPETINYRT FKPEKDGLFC EKIFGPTKDY
ECACGKYKGK KYEGTVCERC GVRVESKEAR RRRMGHIDLV APVVHVWYLK SSPSILSSLL
GIPAKELENV VYYGGKRIIE KILIVTDPKN TDFIKGSQLY QTEYEIYSQK LDFEVVPGVI
IKSPSTPVTS SISGEVKIRH EKTHTDREIT WVDVRKISRA EHRLYTGMIL NVKNGDKVNQ
GDEIVSEMQI DPIYAPFDGT VEIDEISESI TVRPLSTSKD IPVTFSLPYG VKPTVSNGAK
VKKGDQLTNG TVLPAVVASV SGTISFGKDL NVRPREDGKY EVLKNGTLFV ENVVEEKHYP
LFEGALIYVE DGQEINEGDV IADRFLFEDE YLTIDEFKIF EEHYPAMFTA ESEVENDRPI
VVITKIDDEV SVETGLKIGD IITDDQYWAY RVLYGEKIEA DSGAAAIKKL LQNLDLEKLK
AEIEAELKKV SKSSGRAKKL LRRLKIVKDL LKSETKPEWM VLEAIPVVPP DIRPMIQVEG
GRFATTDLND LYRRVINRNN RLKKLYEMNS PEIIIKNEKR MLQEAVDSLI YNGRMGKAVT
DRNGRPLKSL TDLLKGKKGR FRRNLLGKRV DYSGRAVIVV GPHLKIHECG LPKKMAMELF
KPFVLAELLN KDDETSKTAR KMKKAIIEKE LPQAYEVLEE IIKGHPVLLN RAPTLHRMSL
QAFEPRLIEG NAIQLHPLVC PPFNADFDGD QMAVHVPLSA AAQAEAKFLM LSRYNIISPA
HGKPISMPGK DIVAGVYYLT MVDKNFDSVK EKDIKWKFSS IEEAGLAYEF GYIKLHDPIL
VKVDDKVIKT TYGRLIFASI VPDEFKDYNK TYGKGAIKDL VYNTFKKYGV DRTADLLDDI
KDLGFHYATI SGLTVSITDF YISPEREKII EQAKAKVSEI EELFAEGFLS DEERYRETIK
IWADATEKVQ DATFEYIGKD PFNPIYIMVD SGARGNKDQL KQLAGMRGLM ADPSGRTIEI
PIISNFREGL SVLEFFISTH GARKGSADTA LRTSSAGYLT RRLVDVAQSV VVTTTDCGTH
NGVRATVLKS SDGLTVEKLE DFLFGRVLAK DVFDPKTNNV LVNPETGKQY TRDTIIDDDD
AKFLGNYSVR IPVVTEGEID LSSPELPESY CELAEDFVYN DVHYEVGTEV NWDVVRKATS
AGLSKLKVKI YPVVGKVSVE TVLSSKDSKQ LVVDEELIEV TTAKILEENN VESVQVRPEI
IVRSVLTCEA EHGVCSKCYG MDLSNHQIVG VGESVGVVAA QSIGEPGTQL TMRTFHTGGI
ATTADITQGL PRAEELFEAR KKLKEPEGVF SRVKGYVKDI VEDETGRKKV YIEDEAGDIH
EYEIPIKVKV AVNKGQKVLP GQSLSTGAIR PRKILETLDV DATALYLLKE IKKVYVEQGV
DIHDKHFEII IKQMLDKVEV VDPGDTDYLP GDLVRLETVK RINKEILESN VQVDSNRKRV
IGKELHHHLI AEDENGQIVE IAKEGEEVTE EILEKAIKLG IKDLVVKNGE GEIVTYQILP
KEPIKYRRRL LRITKASLER VGWLSAASFQ QTPQVLTEAA IEGAEDLLLG LKENVIVGQL
IPAGTGLDMF ANIQIEETPR FAQEKEKMA
