RPOC_BRUSU
ID RPOC_BRUSU Reviewed; 1400 AA.
AC Q8G070; G0KAG3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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};
GN OrderedLocusNames=BR1242, BS1330_I1238;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN30161.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18579.1; -; Genomic_DNA.
DR RefSeq; WP_004690918.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8G070; -.
DR SMR; Q8G070; -.
DR EnsemblBacteria; AEM18579; AEM18579; BS1330_I1238.
DR GeneID; 45052275; -.
DR KEGG; bms:BR1242; -.
DR KEGG; bsi:BS1330_I1238; -.
DR PATRIC; fig|204722.22.peg.605; -.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR PhylomeDB; Q8G070; -.
DR Proteomes; UP000007104; Chromosome I.
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; 1.
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..1400
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067718"
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 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 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 892
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"
SQ SEQUENCE 1400 AA; 155601 MW; 74EEF72A86A10C3E CRC64;
MNQEVMNLFN PQAPAQTFDS IRISIASPEK ILSWSYGEIK KPETINYRTF KPERDGLFCA
RIFGPIKDYE CLCGKYKRMK YKGIICEKCG VEVTLSRVRR ERMGHIELAA PVAHIWFLKS
LPSRIGTLLD MTLKDIERVL YFENYIVTEP GLTSLKEHQL LSEEEYMIAV DEFGEDQFTA
LIGAEAIYEL LASMELEKIA ADLRVDLAET TSDLKQKKLM KRLKIVENFL ESGNRPEWMI
MKIVPVIPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLIELRAP GIIIRNEKRM
LQEAVDALFD NGRRGRVITG ANKRPLKSLS DMLKGKQGRF RQNLLGKRVD YSGRSVIVTG
PELKLHQCGL PKKMALELFK PFIYARLDAK GYSSTVKQAK KLVEKERPEV WDILDEVIRE
HPVLLNRAPT LHRLGIQAFE PTLIEGKAIQ LHPLVCTAFN ADFDGDQMAV HVPLSLEAQL
EARVLMMSTN NILHPANGAP IIVPSQDMVL GLYYLSIVAE KEPGEGMIFA DMGELQHALE
NKVVTLHTKI KGRFKTVDAE GNPVSKIYDT TPGRMIMGEL LPKNVNVPFD ICNQEMTKKN
ISKMIDHVYR HCGQKETVIF CDRIMQLGFA HACRAGISFG KDDMVIPESK AKIVAETEAL
TTEYEQQYND GLITQGEKYN KVVDAWGKAT DKITEEMMAR LKAVEFDPVT GRQKQMNSVY
MMSHSGARGS VNQMRQLGGM RGLMAKPSGE IIETPIISNF KEGLTVNEYF NSTHGARKGL
ADTALKTANS GYLTRRLVDV AQDAIISEVD CGAEIGLTMQ PIVDAGQIVA SIGQRVLGRT
ALDPILHPVT GEVIVEAGRM IEEKDVEIIE KAGIQSIRIR SALTCETRDG VCAKCYGRDL
ARGTPVNQGE AVGVIAAQSI GEPGTQLTMR TFHLGGTAQV VDSSYLEASY EGTVKLRNRN
VVRNSDGNLV VMGRNMAVLI LDATGKERAV HRVTYGSRLF VDEGDTVKRG QRIAEWDPYT
RPIMTEVEGY VEFEDLVDGL SVSETADEST GITKRVVIDW RSTPRGSDLK PAMVIKDKAG
KILKLSKGGD ARFLLSVESI LSVEPGAHVK AGDVIARLPM ESAKTKDITG GLPRVAELFE
ARRPKDHAII AEIDGTVRFG RDYKNKRRII IEPNDDTIEP VEYLIPKGKP FHLQDGDVIE
KGEYILDGNP APHDILAIKG VEALASYLVN EIQEVYRLQG VLINDKHIEV IVRQMLQKVE
ITESGDTGYI PGDHVDRIEL EEINERLIEE GKKPGSGNPV LLGITKASLQ TPSFISAASF
QETTRVLTEA AVAGKMDTLQ GLKENVIVGR LIPAGTGGMT NQIRRIATAR DELIIDERRK
TSGSAEANAM LVDMTNNAAE
