RPOC_THIDA
ID RPOC_THIDA Reviewed; 1398 AA.
AC Q3SLQ5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Tbd_0399;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ96352.1; -; Genomic_DNA.
DR RefSeq; WP_011310912.1; NC_007404.1.
DR AlphaFoldDB; Q3SLQ5; -.
DR SMR; Q3SLQ5; -.
DR STRING; 292415.Tbd_0399; -.
DR PRIDE; Q3SLQ5; -.
DR EnsemblBacteria; AAZ96352; AAZ96352; Tbd_0399.
DR KEGG; tbd:Tbd_0399; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008291; 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..1398
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225585"
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 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1398 AA; 153693 MW; 15D94F6510F3604C CRC64;
MKALLDLFKQ ATHEEEFDAI KIGLASPDKI RSWSYGEVKK PETINYRTFK PERDGLFCAK
IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTLSKVRRE RMGHIELASP VAHIWFLKSL
PSRLGMVLDM TLRDIERVLY FEGFVVVEPG MTPLNRGQLL TEEDYLGKLE EYGDEFKALM
GAEGVRELLR SLDVASEVET LHSEISKTGS DTKLKKLSKR LKILEGFQKS GIKPEWMILE
VLPVLPPELR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLELKAPEI IVRNEKRMLQ
EAVDSLLDNG RRGKAMTGAN KRPLKSLADM IKGKSGRFRQ NLLGKRVDYS GRSVIVVGPT
LKLHQCGLPK KMALELFKPF IFNRLEVLGL ATTIKAAKKM VEDEEPIVWD LLEEVIREHP
VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAFNAD FDGDQMAVHV PLSLEAQAEA
RTLMLASNNV LSPANGEPII VPSQDIVLGL YYMTREKVNA KGEGMMFADV TEARRAYDNR
EAELHARVTV RIKEVTLDEN KNRVETVKRV ETTLGRALLS EILPPGLPFS FVDKALKKKE
ISKLINASFR RCGLRETVIF ADKLMYTGFT FATRAGMSIA IKDMLIPQEK GQILGAAEAE
VKEIESQYTS GLVTQGERYN KVVDIWGRAG DAVAKAMMGQ LGGEKVTDRQ GKEVTQESFN
AIYMMADSGA RGSAAQIRQL AGMRGLMAKP DGSIIETPIT ANFREGLNML QYFISTHGAR
KGLADTALKT ANSGYLTRRL VDVTQDLVVT EDDCGTKNGL LVKALVEGGE VVEALRERIL
GRVAASDIIN PETQETVFEA GTLLSEDVVD TIEALGIDEV RVRTPLTCET RYGLCANCYG
RDLGRGYLVN VGEAVGVIAA QSIGEPGTQL TMRTFHIGGA ASRAAAASQL EAKSNGAVQY
TATMRYVTNA RKELVAISRS GEILIADDSG RERERHKVPY GATLMVTDGA KIKAGAVLAT
WDPHTRPIIT EYAGRVRFEN VEEGVTVAKQ VDDVTGLSTL VVIDPKRKST STKGVRPQVK
LLDDAGNELK IAGTDTLVNI TFQIGSIITV KDGQDVAVGD VLARIPQETS KTRDITGGLP
RVAELFEARS PKDAGVLAEV TGTVSFGKDT KGKQRLVITD LDGVAHEYLI TKEKHVTAHD
GQIVQKGEMI VDGPVDPHDI LRLQGVEALA SYITDEVQDV YRLQGVKIND KHIEVIVRQM
LRRVVVADPG DTGLIPGEQV ERSEVLQIND EMIAAGKEPA VYDPILLGIT KASLSTDSFI
SAASFQETTR VLTEAAIMGK KDELRGLKEN VIVGRLIPAG SGLAYHNTRR RQAAGEDMGA
DRLLEGGETP AAENQEVA
