RPOC_NITEC
ID RPOC_NITEC Reviewed; 1404 AA.
AC Q0AF54;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Neut_1794;
OS Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=335283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101675 / C91 / Nm57;
RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT eutropha C91: implications for niche adaptation.";
RL Environ. Microbiol. 9:2993-3007(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}.
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; CP000450; ABI60028.1; -; Genomic_DNA.
DR RefSeq; WP_011634834.1; NC_008344.1.
DR AlphaFoldDB; Q0AF54; -.
DR SMR; Q0AF54; -.
DR STRING; 335283.Neut_1794; -.
DR PRIDE; Q0AF54; -.
DR EnsemblBacteria; ABI60028; ABI60028; Neut_1794.
DR KEGG; net:Neut_1794; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001966; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1404
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353397"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 825
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1404 AA; 155338 MW; 61C40F3B1DDD8867 CRC64;
MKALLDLFKQ VTQKEEFDSI KIGLASPEKI RSWSYGEVKK PETINYRTFK PERDGLFCAK
IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTLSRIRRE RMGHIELASP VAHIWFLKSL
PSRLGLVLDI TLRDIERVLY FEAYIVTDPG MTPLTRGQLL TEDDYLNKTE EFGDDFSAAM
GAEGIRALLN SMDILSEIES LRLEIQTTGS ETKIKKAAKR LKVLEAFNKS GMKPEWMILT
VLPVLPPELR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLELRAPEI IIRNEKRMLQ
ESVDSLLDNG RRGKAMTGAN KRPLKSLADM IKGKGGRFRQ NLLGKRVDYS GRSVIVVGPQ
LKLHQCGLPK KMALELFKPF IFNKLEVMGV ASTIKAAKRE VENENPIVWD ILEEVIREHP
VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAFNAD FDGDQMAVHV PLSLEAQMEC
RTLMLSTNNV LSPANGDPII VPSQDIVLGL YYMTREKVGA QGEGMVFSDV SEITRAYESK
ALELNARITV RIKEKKKSCG HGEDPIETIT RFETTVGRAL ISEILPAGLP FALVNKTLKK
KEISKLINAS FRLCGLRETV IFADKLMYSG FSYATRGGIS ICLDDLVTPS QKTGIIQAAE
QEIHEIANQY ISGLVTQGER YNKVVDIWAR AGDQVAKAMM DQLSVEPVKD QETGEIRTDK
NGQAVTQESF NSIYMMADSG ARGSAAQIRQ LSGMRGLMAK PDGSIIETPI TANFREGLNI
LQYFISTHGA RKGLADTALK TANSGYLTRR LVDVTQDLVI IENDCGTDGG VVMKALVEGG
NVVESLRGRI LGRVAATDVI NPETGEVICS EGTLLDEDTA DEIEACSVDE VKVRTPLTCE
TRYGLCAKCY GRDLGRGTPV NVGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASRAVVANQ
AESKSNGVVR YSHHIRYVKN AQNELIIISR SGEILIQDEN GRERERHKIP YGATLHVQDG
ETIKAGQILG SWEPHKRPII TEYAGKIRFE NVEEGVTVVR QIDEITGMAT LVVIDPKRRN
IAQSKGLRPL VKFLDENDQE INIPGTDQPV SITFHVGSII TVRDGQQVGI GEVLARIPQE
TSKTRDITGG LPRVAELFEA RVPKDAGFLA EATGTVAFGK DTKGKQRLVI TDLDGIAHEY
LIPKDKHVTA HDGQVVNKGE VIVDGPIDPH DILRLQGVEA LAKYISDEVQ DVYRLQGVSI
NDKHIEVIVR QMLRRVQITN AGDSAFILGE QVERAEVLAE NEKLITENKM PATYEYVLLG
ITKASLSTDS FISAASFQET TRVLTEASIM GKKDDLRGLK ENVIVGRLIP AGTGLSFHNI
RKKQRLSEST VYLDADLTEN EIAE
