ID   RPOB_STAAW              Reviewed;        1183 AA.
AC   P60279; Q99W65;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, 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=MW0497;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB94362.1; -; Genomic_DNA.
DR   RefSeq; WP_000918667.1; NC_003923.1.
DR   AlphaFoldDB; P60279; -.
DR   SMR; P60279; -.
DR   EnsemblBacteria; BAB94362; BAB94362; BAB94362.
DR   KEGG; sam:MW0497; -.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000418; 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_0000047963"
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