RPOC_NITSB
ID RPOC_NITSB Reviewed; 1507 AA.
AC A6Q1M4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=NIS_0269;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF69383.1; -; Genomic_DNA.
DR RefSeq; WP_012081646.1; NC_009662.1.
DR AlphaFoldDB; A6Q1M4; -.
DR SMR; A6Q1M4; -.
DR STRING; 387092.NIS_0269; -.
DR PRIDE; A6Q1M4; -.
DR EnsemblBacteria; BAF69383; BAF69383; NIS_0269.
DR KEGG; nis:NIS_0269; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001118; 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; -; 1.
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; 1.
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 TIGRFAMs; TIGR02386; rpoC_TIGR; 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..1507
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308867"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 800
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 874
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 881
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1507 AA; 168274 MW; D37A73A887165A8C CRC64;
MKKLVPIEIG EEKRPKDIKA IQFRLASPEK ILSWSHGEVK KPETINYRTL KPERDGLFCA
KIFGPIKDYE CLCGKYKKMR YKGVVCEKCG VEVTTSKVRR SRMGHIELVT PVAHIWYVNS
LPSRIGTLLG VKMKDLERVL YYEAYIVKNP GEAYYDFEKK NPVKKYDVLN EEQYQQLVQH
FGDTGFDARM GGEVVKELLE EFDLVEAFEQ LREEMKNTNS EAKRKTIVKR LKVIESFLNS
GNRPEWMMLT VVPVLPPDLR PLVALDGGKF AVSDVNDLYR RVINRNQRLK RLLELDAPEI
IVRNEKRMLQ EAVDALIDNG RRGNAVKGAN KRPLKSLSEI IKGKQGRFRQ NLLGKRVDFS
GRSVIVVGPN LRMDQCGLPK LMALELFKPH LLAKLEEKGY ATTLKQAKKM IEDRENVVWE
CLQEIVDEYP VLLNRAPTLH KLSIQAFHPV LIDGKAIQLH PLVCSAFNAD FDGDQMAVHV
PLTEEAIAEC KILMLSSMNI LLPASGRAIA VPTQDMVLGI YYLSKEKEDA KGTHKLFADI
NEVMTALESD YLDLNAKIRT KIDNQVIYTT AGRLIIKSIL PDFVPVNLWN KVLKKKDIAN
LVDYVFKEGG PKITAEFLDN LKELGFKYST VTGISISAYD IKVPDSKKRL IEEAKRKVKE
IQQQFQAGLL TEQERYNKII DIWTDTSNEV AKEMMELMKN DKDGFNSVYM MADSGARGSS
AQIRQLAGMR GLMAKPDGTI IETPIISNFK EGLNVLEYFI STHGARKGLA DTALKTANAG
YLTRKLVDVA QNVKITMDDC GTHEGVEITD ISVGNELIEP LEDRIFGRVL AQDIMDPITN
EILFSEGTLL DEEKTRKIIE AGIKSVTIRT PITCKAEKGV CAKCYGLNMA EGKLVKPGEA
VGIIAAQSIG EPGTQLTLRT FHVGGTASRS AEERQVVATK EGFIRYYNLK TYETEDGKII
VANRRNAAVL LVEPKIKALF NGEIEVKPIH DEVLITLSNG EEKVRYSFKK SDFARPNELA
GVSGKIEGKL YLPYESGTKV EAGESIVEII KEGWNIPNRI PYAAILKVKD GAPVTQKIVS
GAKGVVKYYK LKGDYLERFE GVKEGEKIEE KGLFAVIADE EGREAARHYI ARGSIIEVAD
DQSVDKDTVI AMPAKSDKTV IAEWDPYSIP IIAEKEGVIT FEDIIPGVTA VEQVDEFTGE
TRLTINEYIP AEYKPAIVLA PKDGSEIIRY VLDPKTAIYV QNGQEVKLAQ TLAKTPKAAA
KSKDITGGLP RVSELFEARR PKDPAVVAEI DGVVSFGKPS RGKQRIIITA DTGQTVEYLI
DKNRQILVHN GEFVHAGERL TDGTVSGHDI LRTLGEKALM YYMVSEIQQV YRRQGVNISD
KHIEIIVSQM LRQVKIVDSG DTKFIPGDLV SKKEFRKENE KILRLGGQPA IAEPILIGIT
RAAVSSDSVI SAASFQDTTK VLTEASVSAK VDHLEDLKEN VIIGRLIPVG TGLYKDRKVK
VETASQE
