RPOB_STAA8
ID RPOB_STAA8 Reviewed; 1183 AA.
AC P47768; Q2G0N6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321};
GN OrderedLocusNames=SAOUHSC_00524;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7772603; DOI=10.1016/0167-4781(95)00054-k;
RA Aboshkiwa M.A., Rowland G., Coleman G.;
RT "Nucleotide sequence of the Staphylococcus aureus RNA polymerase rpoB gene
RT and comparison of its predicted amino acid sequence with those of other
RT bacteria.";
RL Biochim. Biophys. Acta 1262:73-78(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 379-460 AND 538-622.
RX PubMed=1402788; DOI=10.1099/00221287-138-9-1875;
RA Aboshkiwa M.A., Coleman G., Rowland G.C.;
RT "Cloning and physical mapping of the Staphylococcus aureus rplL, rpoB and
RT rpoC genes, encoding ribosomal protein L7/L12 and RNA polymerase subunits
RT beta and beta'.";
RL J. Gen. Microbiol. 138:1875-1880(1992).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
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_01321};
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_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD29672.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X64172; CAA45512.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29672.1; ALT_INIT; Genomic_DNA.
DR PIR; S59951; S59951.
DR RefSeq; WP_000918667.1; NZ_LS483365.1.
DR RefSeq; YP_499096.2; NC_007795.1.
DR AlphaFoldDB; P47768; -.
DR SMR; P47768; -.
DR STRING; 1280.SAXN108_0596; -.
DR EnsemblBacteria; ABD29672; ABD29672; SAOUHSC_00524.
DR GeneID; 3920377; -.
DR KEGG; sao:SAOUHSC_00524; -.
DR PATRIC; fig|93061.5.peg.470; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR PRO; PR:P47768; -.
DR Proteomes; UP000008816; 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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1183
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047964"
FT CONFLICT 797..798
FT /note="EA -> RRQ (in Ref. 1; CAA45512)"
FT /evidence="ECO:0000305"
FT CONFLICT 1180..1183
FT /note="EVTD -> SY (in Ref. 1; CAA45512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1183 AA; 133219 MW; 54B545295DC01D1A CRC64;
MAGQVVQYGR HRKRRNYARI SEVLELPNLI EIQTKSYEWF LREGLIEMFR DISPIEDFTG
NLSLEFVDYR LGEPKYDLEE SKNRDATYAA PLRVKVRLII KETGEVKEQE VFMGDFPLMT
DTGTFVINGA ERVIVSQLVR SPSVYFNEKI DKNGRENYDA TIIPNRGAWL EYETDAKDVV
YVRIDRTRKL PLTVLLRALG FSSDQEIVDL LGDNEYLRNT LEKDGTENTE QALLEIYERL
RPGEPPTVEN AKSLLYSRFF DPKRYDLASV GRYKTNKKLH LKHRLFNQKL AEPIVNTETG
EIVVEEGTVL DRRKIDEIMD VLESNANSEV FELHGSVIDE PVEIQSIKVY VPNDDEGRTT
TVIGNAFPDS EVKCITPADI IASMSYFFNL LSGIGYTDDI DHLGNRRLRS VGELLQNQFR
IGLSRMERVV RERMSIQDTE SITPQQLINI RPVIASIKEF FGSSQLSQFM DQANPLAELT
HKRRLSALGP GGLTRERAQM EVRDVHYSHY GRMCPIETPE GPNIGLINSL SSYARVNEFG
FIETPYRKVD LDTHAITDQI DYLTADEEDS YVVAQANSKL DENGRFMDDE VVCRFRGNNT
VMAKEKMDYM DVSPKQVVSA ATACIPFLEN DDSNRALMGA NMQRQAVPLM NPEAPFVGTG
MEHVAARDSG AAITAKHRGR VEHVESNEIL VRRLVEENGV EHEGELDRYP LAKFKRSNSG
TCYNQRPIVA VGDVVEYNEI LADGPSMELG EMALGRNVVV GFMTWDGYNY EDAVIMSERL
VKDDVYTSIH IEEYESEARD TKLGPEEITR DIPNVSESAL KNLDDRGIVY IGAEVKDGDI
LVGKVTPKGV TELTAEERLL HAIFGEKARE VRDTSLRVPH GAGGIVLDVK VFNREEGDDT
LSPGVNQLVR VYIVQKRKIH VGDKMCGRHG NKGVISKIVP EEDMPYLPDG RPIDIMLNPL
GVPSRMNIGQ VLELHLGMAA KNLGIHVASP VFDGANDDDV WSTIEEAGMA RDGKTVLYDG
RTGEPFDNRI SVGVMYMLKL AHMVDDKLHA RSTGPYSLVT QQPLGGKAQF GGQRFGEMEV
WALEAYGAAY TLQEILTYKS DDTVGRVKTY EAIVKGENIS RPSVPESFRV LMKELQSLGL
DVKVMDEQDN EIEMTDVDDD DVVERKVDLQ QNDAPETQKE VTD