RPOC_NITEU
ID RPOC_NITEU Reviewed; 1404 AA.
AC Q82T76;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=NE2045;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD85956.1; -; Genomic_DNA.
DR RefSeq; WP_011112558.1; NC_004757.1.
DR AlphaFoldDB; Q82T76; -.
DR SMR; Q82T76; -.
DR STRING; 228410.NE2045; -.
DR PRIDE; Q82T76; -.
DR EnsemblBacteria; CAD85956; CAD85956; NE2045.
DR KEGG; neu:NE2045; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR PhylomeDB; Q82T76; -.
DR Proteomes; UP000001416; 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 InterPro; IPR011054; Rudment_hybrid_motif.
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 SUPFAM; SSF51246; SSF51246; 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..1404
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067769"
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; 155851 MW; 6F91DD8B6D9542E0 CRC64;
MKALLDLFKQ VTQKEEFDSI KIGLASPEKI RSWSYGEVKK PETINYRTFK PERDGLFCAK
IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTLSRIRRE RMGHIELASP VAHIWFLKSL
PSRLGLVLDM TLRDIERVLY FEAYVVTDPG MTPLNRGQLL TEDDYLNKTE EFGDDFSAVM
GAEGIRTLLS NMDIPLEIES LRLEIQTTGS ETKIKKAAKR LKVLEAFNKS GMKPEWMILT
VLPVLPPELR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLELRAPEI IIRNEKRMLQ
ESVDSLLDNG RRGKAMTGAN KRPLKSLADM IKGKGGRFRQ NLLGKRVDYS GRSVIVVGPQ
LKLHQCGLPK KMALELFKPF IFNKLETMGV ASTIKAAKRE VENESPIVWD ILEEVIREHP
VMLNRAPTLH RLGIQAFEPI LVEGKAIQLH PLVCAAFNAD FDGDQMAVHV PLSLEAQMEC
RTLMLSTNNV LSPANGDPII VPSQDIVLGL YYMTRKKIGA QGEGMVFSDI SEVVRAYENK
VVELNAGIIV RIKERKKSRS HGEEPVEAIT RYETTVGRAL ISEILPAGLP FSIINKVLKK
KEISKLINAS FRLCGLRETV IFADKLMYSG FSYATRGGIS ICLDDLVTPS QKNDIIHAAE
QEVHEIANQY ISGLVTQGER YNKVVDIWGR AGDQVAKAMM DQLSVEPVTD RETGQVRADK
NGQVVTQESF NSIYMMADSG ARGSAAQIRQ LSGMRGLMAK PDGSIIETPI TANFREGLNI
LQYFISTHGA RKGLADTALK TANSGYLTRR LVDVTQDLVI TEDDCDTDGG VIMKALVEGG
DVIESLRERI LGRVAATDIV NPETGAVIYA AGMLLDEDAV DEIETCGIDE VKVRTPLTCE
TRYGLCAKCY GRDLGRGMLV NVGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASRTVVANQ
VESKSNGVIR YSHHIRYVKN AQNELIVISR SGEVYIQDEN GRERERHKIP YGATLLVQDG
EVIKAGQILA SWEPHKRPII AEYAGKVRFE NVEEGVTVVR QIDEITGLAT LVVIDPKRRN
VAQSKGLRPL VKFLDENDNE INIPGSDQPV SITFHVGSII TVRDGQQVNI GEVLARIPQE
TSKTRDITGG LPRVAELFEA RVPKDVGFLA EATGTVAFGK DTKGKQRLVI TDLDGVAHEY
LIPKDKHVTA HDGQVVNKGE VIVDGPIDPH DILRLQGVEA LARYISNEVQ DVYRLQGVRI
NDKHIEVIVR QMLRRVQIMN AGDSSFIPGE QVERAEVLTE NEKLIAENKM PATYEYVLLG
ITKASLSTDS FISAASFQET TRVLTEASIM GKKDDLRGLK ENVIVGRLIP AGTGLSFHNI
RKKQRLSESA AYLDTDLTEN EVTE
