RPOC_BLOFL
ID RPOC_BLOFL Reviewed; 1420 AA.
AC Q7VRP8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Bfl556;
OS Blochmannia floridanus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=203907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(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; BX248583; CAD83238.1; -; Genomic_DNA.
DR RefSeq; WP_011126814.1; NC_005061.1.
DR AlphaFoldDB; Q7VRP8; -.
DR SMR; Q7VRP8; -.
DR STRING; 203907.Bfl556; -.
DR PRIDE; Q7VRP8; -.
DR EnsemblBacteria; CAD83238; CAD83238; Bfl556.
DR KEGG; bfl:Bfl556; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002192; 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..1420
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067724"
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 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
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 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 903
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"
SQ SEQUENCE 1420 AA; 158450 MW; 686348F8169C6DDA CRC64;
MKDLFKFFKT HSNGKIEEFN TIKIQLASPD MIRSWSFGEV KKPETINYRT FKPERDGLFC
SRIFGPIKDY ECLCGKYKRL KHRGVVCEKC GVEVTQSKVR RERMGHIELA SPTAHIWFLK
SLPSRIGLLL DMPLRDIERV LYFESYVVVE GGMTSLECRQ ILTEEEYLDA LEEFGDEFEA
KMGAEAIQIL LKNMDLKNEC ECLRAFLEDS HSETKRKKVS KRIKLIESFI LSNNKPEWMI
LNVLPVLPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLLDLSAP EIIVRNEKRM
LQEAVDALLD NGRRGRAITG ANKRPLKSLA DMIKGKQGRF RQNLLGKRVD YSGRSVITVG
PYLKLHQCGL PKKMALELFK PFIYGQLELK GLASTIKAAK KMVDREESVV WDILEDVIKE
HPVMLNRAPT LHRLGIQAFE PILIEGKAIQ LHPLVCAAYN ADFDGDQMAV HVPLTLEAQL
EARALMMSTN NILSPANGEP IIVPSQDVVL GLYYMTRDRI NSKGEGMVLS NPKEAERLYR
LGIAELHARV KVRITEYKLD NHGRWVDKIN FVNSTIGRAI FWMIVPKGLS FDLVNKVLGK
KSISMMLNHC YRVLGLQSTV MFADQIMYTG FTYAARSGAS VGIDDMIIPT KKVDIIDAAE
SEVAEIQEQF QTGLVTAGER YNKVIDIWAS ANERVSKAMM DNLATETVIN SHGLLETQAS
FNNIFMMADS GARGSAAQIR QLAGMRGLMA KPDGSIIETP ITANFREGLN VLQYFISTHG
ARKGLADTAL KTANSGYLTR RLVDVAQDLV ITQDDCNTFA GIVMSAIIEG GDVKESLRER
VLGRVLAEDI LKSSNDSDVS NSEVLIKRNI LLDEFYCDIL DEYLIDVVKV RSVVTCDTDF
GVCAKCYGRD LARGKLVNKG EAIGVIAAQS IGEPGTQLTM RTFHIGGAAS RVASESSIQI
KNQGIVRLKN VKAVINGQGK LVITSRHAEL KIVDQFDRAK ESYKIPYGSI VMKKDGELAV
SGEIVAYWDP HTMPVIAEVS GFVKFIDMVD GQSVIHQTDD LTGLTSIVVL DTSERVSSAK
DLRPTLKIID VNGYDIFIPG TDISAQYFLP GKSVIQLVDG SRIISGDVLA RLPHETSGTK
DITGGLPRVA DLFEARRPKE AAILAEISGV ISFGKETKGK RRLMICSTDE NGGENIYEEM
IPKWRHLNVF EGEYVERGDV ISDGPESPHD ILRLRGVHAV TNYIVNEVQE VYRLQGVKIN
DKHIEVIIRQ MLRKAIVIRS GDSDFLAGEQ VEYARIKIVN QTLEREGKVK VSFVRNLLGI
TKASLATESF ISAASFQETT RVLTESSVAG KKDDLRGLKE NVIVGRLIPA GTGYAYHQKR
ILKRYSESYS DSKLKENLIE TIPVTADEAS ANLTELLNAT
