RPOC_SULDN
ID RPOC_SULDN Reviewed; 1503 AA.
AC Q30TP6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Suden_0354;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/aem.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
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; CP000153; ABB43635.1; -; Genomic_DNA.
DR RefSeq; WP_011371989.1; NC_007575.1.
DR AlphaFoldDB; Q30TP6; -.
DR SMR; Q30TP6; -.
DR STRING; 326298.Suden_0354; -.
DR PRIDE; Q30TP6; -.
DR EnsemblBacteria; ABB43635; ABB43635; Suden_0354.
DR KEGG; tdn:Suden_0354; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002714; 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; 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..1503
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240829"
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 1503 AA; 166266 MW; DA197E3E7CAEFB4B CRC64;
MSKLVPIEVT EDRRPTDIKQ IQFRLASPEK VMSWSHGEVK KPETINYRTL KPERDGLFCA
KIFGPVRDYE CLCGKYKKMR YKGVVCEKCG VEVTSTKVRR IRMGHIELVT PVAHIWYVSS
LPSRIGTLLG IKMKDLERVL YYEAYIVESG GEAYYDAEAK TPVLKYDVLN EEQYRTLVSR
FGELGFKARM GGEVVRDLLD SIDLVDLFTQ LKEDIELTKS EAKTKTIAKR LKVIESFLNS
GNNPAWMMLT VLPVLPPDLR PLVSLDGGKF AVSDVNDLYR RVINRNQRLK RLVELEAPEI
IVRNEKRMLQ ESVDALFDNG RRANAVKGAN KRPLKSLSEI IKGKQGRFRQ NLLGKRVDFS
GRTVIVVGPS LSMDECGLPK KMALELFKPH LIAKLEDKGY ATTVKAAKKM IEDKTNEVWE
CLAEIVDGYP VLLNRAPTLH KLSIQAFHPK LIDGKAIQLH PLVCAAFNAD FDGDQMAVHI
PLSSAAIAEA KVLMLASMNI LLPASGKAIA TPSQDMVLGI YYITLEKNGV KGSNKLFANV
DEVRIAIEHD ALDIHAKVRT RDDGRIIHTT AGRMLLKAIL PNFVPSELWN RVMKKKAINE
VVDYVQKHGG IGVTAGFLDR LKNLGFKHAT EAGISISIDD IKIPAGKEAK IAESKNRVFE
IQKQFEAGLL TEQERYNKII DVWTDTNNTL ATQMMDLVQT DKAGFNSIHM MADSGARGSA
AQIRQLAGMR GLMAKPSGEI IETPIISNFK EGLNVVEYFI STHGARKGLA DTALKTANAG
YLTRKLVDVA QNVKIVEHDC HTHEGIEISD ISDQNTLIES LEDRLNGRVL ADDVIDPISN
EILFAEGTLL DEVSAKVIAE AGIKTAYIRT PTTCKSENGI CALCYGVNLA TGQIVRRGEA
VGIIAAQSIG EPGTQLTLRT FHVGGTASST AQERQVVAEK EGFIRYYNLK TYVSKEGRNI
VANRRNAAVL LVEPKIKAPF SGRVEIQTVH DEVIISVSSK TDTIRYVLRK NEIAKPNELA
GVGGQIEGKY YFPYESGAEV QEYESIVETI KDGWNVPSRI PYASEVLVAN GAPVTQKIFA
KEDGVVKYFL LRGDYLERFE GLKAGYEVIE KGLFATVVDS NNREAVRHYI ARGSIIVAED
DAVVDPKTLI AKPKNDESTV IAEWDPYSNP IISETSGTVK FEDIIIGTTA TEQYDELTGK
TRLMISDHVP AEYKPTIVLA SEDGELLRYQ VQSKTSIYVE DGAKVKVADI IAKTPKALQK
SSDITGGLPR VSELFEGRRP KATALISEID GVVSFGKSLR GKIRIIVASD NGILKEYFVD
KSHTPVVNSG DFVHAGERLT SGIISSHELL RIMGVKTLYN YLVSEVQQVY RSQGVNISDK
HIEVIFTQML RQVKILKSGD TKFIEGDLIS KVKFAQENEK IIKLGGRPAI AEPFLVGITR
AAVSADSIIS AASFQDTTKV LTEAAVSAKV DDLNDLKENV IIGRTIPVGT GIYKDQEIMF
GYN
