RPOB_STAES
ID RPOB_STAES Reviewed; 1183 AA.
AC Q8CQ84;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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}; OrderedLocusNames=SE_0306;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(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_01321}.
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}.
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DR EMBL; AE015929; AAO03903.1; -; Genomic_DNA.
DR RefSeq; NP_763861.1; NC_004461.1.
DR RefSeq; WP_001833083.1; NZ_WBME01000014.1.
DR AlphaFoldDB; Q8CQ84; -.
DR SMR; Q8CQ84; -.
DR STRING; 176280.SE_0306; -.
DR EnsemblBacteria; AAO03903; AAO03903; SE_0306.
DR GeneID; 50019529; -.
DR KEGG; sep:SE_0306; -.
DR PATRIC; fig|176280.10.peg.281; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001411; 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; Transcription;
KW Transferase.
FT CHAIN 1..1183
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047965"
FT REGION 1151..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1183 AA; 133039 MW; BEFE7454FFF67857 CRC64;
MAGQVVQYGR HRKRRNYARI SEVLELPNLI EIQTKSYDWF LKEGLLEMFR DISPIEDFTG
NLSLEFVDYR LGEPKYDLEE SKNRDATYAA PLRVKVRLII KETGEVKEQE VFMGDFPLMT
DTGTFVINGA ERVIVSQLVR SPSVYFNEKI DKNGRENYDA TIIPNRGAWL EYETDAKDVV
YVRIDRTRKL PLTVLLRALG FSTDQEIVDL LGDSEYLRNT LEKDGTENTE QALLEIYERL
RPGEPPTVEN AKSLLYSRFF DPKRYDLASV GRYKANKKLH LKHRLFNQKL AEPIVNSETG
EIVVDEGTVL DRRKLDEIMD VLETNANSEV FELEGSVIDE PVEIQSIKVY VPNDEEGRTT
TVIGNALPDS EVKCITPADI VASMSYFFNL LNGIGYTDDI DHLGNRRLRS VGELLQNQFR
IGLSRMERVV RERMSIQDTD SITPQQLINI RPVIASIKEF FGSSQLSQFM DQANPLAELT
HKRRLSALGP GGLTRERAQM EVRDVHYSHY GRMCPIETPE GPNIGLINSL SSYARVNEFG
FIETPYRKVD LDTNSITDQI DYLTADEEDS YVVAQANSRL DENGRFLDDE VVCRFRGNNT
VMAKEKMDYM DVSPKQVVSA ATACIPFLEN DDSNRALMGA NMQRQAVPLM NPEAPFVGTG
MEHVAARDSG AAITAKHRGR VEHVESNEIL VRRLVEENGT EHEGELDRYP LAKFKRSNSG
TCYNQRPIVS IGDVVEYNEI LADGPSMELG EMALGRNVVV GFMTWDGYNY EDAVIMSERL
VKDDVYTSIH IEEYESEARD TKLGPEEITR DIPNVSESAL KNLDDRGIVY VGAEVKDGDI
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 ESIVKGENIS RPSVPESFRV LMKELQSLGL
DVKVMDEHDN EIEMADVDDE DAAERKVDLQ QKSAPESQKE TTD
