RPOC_THEP1
ID RPOC_THEP1 Reviewed; 1690 AA.
AC A5IJW2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Tpet_0461;
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=390874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
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., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-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; CP000702; ABQ46485.1; -; Genomic_DNA.
DR RefSeq; WP_011943103.1; NC_009486.1.
DR AlphaFoldDB; A5IJW2; -.
DR SMR; A5IJW2; -.
DR STRING; 390874.Tpet_0461; -.
DR EnsemblBacteria; ABQ46485; ABQ46485; Tpet_0461.
DR KEGG; tpt:Tpet_0461; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; EHEIIAN; -.
DR Proteomes; UP000006558; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1690
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353450"
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; 190694 MW; 632F6C3A1C141601 CRC64;
MPMSSFKRKI KAIQIKIASP EVIRSWSGGE VKKPETINYR TFKPERDGLF CERIFGPVKD
YECACGKYKG KKYEGTVCER CGVRVESREA RRKRMGHIEL AAPAVHIWYL ESIPSVLGTL
LNMSTSDLEN IIYYGSRRVI ERAFIVTDPK DTPFSQGDVI YETEYRIYRK KWDFEVEQAF
VVKNPKSPVL SDIDGEVTLK TEKSITGREI TWIIVKNITR ATHTVLPGMI LVVKDGQEVE
KGQDLTKEMT IDPVYAPFDG HVEIDELSNT ITLKPLTTSK DQPVVFTAPY GAKILVSNGQ
KVKKGDQITT STSLPSVKSS 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 HLKIHQCGIP
KKMAMELFKP FVLAKLLGEG SSSKTMRKVK KAIIEKEMPE AWEVLEEVIK GSVVLLNRAP
TLHRMSIQAF EPKLVEGNAI QLHPVVCPPF NADFDGDQMA VHVPLSAAAQ AEARFLMLSR
YNIISPAHGK PISLPTQDII IGSYYLTTVS KEFDSLKEED VKWKFSSPEE AMLAYHLGFI
KLHTPILIKV VINGEEKRIK TTLGRVIFNS ILPEDLRDYN RIFDKKQINT LVYETFKRHG
IDRAADLLDD IKDIGFHYAT VSGLTLSLKD LKIPPERDEI LRKTWEKVRI IEENYEKGFL
TEEQRKSEII RLWMSVTEEI TKLTSRTLAE DPFNPIYMMV NSGARGNIDQ VKQLAGIRGL
MIKAYDPRSR EIKSKIFKGQ AIHEALTFDY PVDKNLREGV DILQFFISTY GARKGQVDTA
MNTSFAGYLT RRLVDVAQSV TVAEPDCGTH EGIRAMDLIK EGTVVEKMNE FLFGRVLAKD
VLDPETKEVL KNPETGKEYT RNTMLTDDDA NFLASYKKMV DVVRYEEIDI TELSLPNMYA
EIAEPVGEYE EGTELTWDVV KAAKNEGKYR IKVKVYPVVG TVYAEEEPLY DKKGERQLLV
YQEVINEIVA KMLEENGIEK VPVRPDIIVR SPLTCESEYG VCAACYGMDL SNHKIVNVGE
SVGIVAAQSI GEPGTQLTMR TFHVGGVMGA SDIVSGLTTV EKTFEPYAFL REEKSGGKKE
IRKYYGSESI LCEVDGFVKD IATDESGRTV IYVEDYAGNI HAYKVPKRAK VRVEKGQKVL
RGETLTSGAI VWWKLLELES EKGVMTAMNL LKIIKNAYVQ QGVSIHDKHF EIIFKQMLSM
ATIVDPGDSD YLPDQLVPLV DIKRFNREIL EGNAKVEENR KWVIGKTLAK RIIAETEEGE
LVELAQKGDE VTEELLKKII EAGIKEIDVF EKDKVVTYQI LPKEPIKYKR RLLSLKKAAL
NYPGWLSAAA FEETAWVLTA AAIEGKVDPL IGLKENVIVG QLIPSGTGLD VFAGIQVEET
PRAAVEEELA
