RPOC_PSELT
ID RPOC_PSELT Reviewed; 1650 AA.
AC A8F4G1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Tlet_0478;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
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., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-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; CP000812; ABV33045.1; -; Genomic_DNA.
DR RefSeq; WP_012002526.1; NC_009828.1.
DR AlphaFoldDB; A8F4G1; -.
DR SMR; A8F4G1; -.
DR STRING; 416591.Tlet_0478; -.
DR PRIDE; A8F4G1; -.
DR EnsemblBacteria; ABV33045; ABV33045; Tlet_0478.
DR KEGG; tle:Tlet_0478; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002016; 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..1650
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353449"
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 747
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 751
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1082
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1650 AA; 184461 MW; 156EC8EA46BEBA65 CRC64;
MAISTFKRKI ASVRVSVASP EIIRAWSSGE VKKPETINYR SFKPERDGLF CEKIFGPTKD
YECACGKYKG KKYEGTVCER CGVRVESKEA RRKKMGHIEL AAPVVHVWYL KSSPSILSTL
LNIPARDLEN IVYHGSRRII ERSYIITDSK KTQFAAGDVL YETEYEVYKK VLDFDAEIAV
TVKNPKSPVV SDIDGEVSIK SEQTNTGREI IWITVKDSKK IPIQLQPGMI LLSKNGQEVK
EGTILVPEKQ IAPFYAPFDG TVEIDEIAST LTIKPLTTSK EQPVTVTIPY CVRVLVKNGS
KVKAADELLS GGTIPAITSP ASGKVVFGKE LNVRPLEDDT YEVLSAGMLY VEQLIQEKRY
PIFEGSLPYV NDGDKVKAGD YLADRFLFED EVLSAHEYKI FEDYYPQQFT VEAEVENDRP
IVAVTEIDDE LSKETGLSVG SIITESEYEA YKELYPGKIE AHYGAAAVKK LLEKIDLEKL
KAQIESELSQ LPRSSGKALK LLKRLKIVKN LIKSGTKPEW MVLEAVPVIP PELRPMIQID
GGRFATTDLN DLYRRVINRN NRLRRLLDLN APDIIVRNEK RMLQESVDSL IYNGRIGKAV
ADRNGRALKS LTDLVKGKKG RFRRNLLGKR VDYSGRAVIV VGPDLKIHQC GLPKKMAMEL
FRPFVLAQLL KEGGESSKTA RKMKKAIIEK EMPEAWDILE EVIKGHPVLL NRAPTLHRMS
IQAFEPKLIE GNAIQLHPLV CPPFNADFDG DQMAVHVPLS AAAQAEAKYL MLSRYNIISP
AHGKPISMPG KDIIVGVYYL TAIGKDFDDV KTEEIRYRFG STEEAILAYS LGYVDLHTPV
LAKVKVSDQE KIVKTTVGRI IFNEIILPDL RDYTRVFGKK EIKNLIYDTF KRHGIDATAD
LLDDMKDLGF HYATVSGLTI SLKDLIVSPK KDEIIRGAEQ RVEQVEEEYR RGFLTFDERY
REIIKIWNKA TEDVQFVTQQ ALGENPFNPI FMMVNSGARG NIDQVKQLAG MRGLMADPSG
KTIEIPIISN FREGLTSMEF FISTHGARKG AADTALRTSS AGYLTRRLVD VAQSIVITTT
DCGTHEGLKA VELISDDLTV QKLKDFLFGR VLSRDVVDPL TGEVIKNPVT GREYVRNAML
SDEDAEFLAE YVVSVPVSVE QVLDLQGLQL PHCYAEVCEE IRTVDGVYYE EGTELNWDVV
RNAKNAGKKQ LKIKMYPVVG TISEQVIKDK KGEKELVVLR EEIDELTAKI LEENGVSQIK
VRPNIYVRSV LTCEAEKGVC AMCYGMDLSN HKVVNVGEAV GIIAAQSIGE PGTQLTMRTF
HTGGIATTAD ITQGLPRAEE LFEARKKLKE PEGIFSTETG FVKDIKEVEG RQKIYIEDYS
GGIHEYEVPE KTKVKVRIGQ KVLPGTPLTT GAIRLRKLMD TLGVEATAMY LLKETQKVYV
EQGVEIHNKH FEIIIKQMLG RVEIVDPGDT DFLPGQLMTI SEAEKINEKI LRENANAQSN
RNFVLGKILA KKVVAKVSDE VEEIASEGTE VTEEILEKAV ESGVKEICIY DEGKQITYQI
APKEPMRYRR RLLRITKASL EQKGWLSAAS FQQTPQVLTE AAVEGSIDLL EGLKENVIVG
QLVPAGTGLE TFANIQIEET PRAAEAEKMA
