ID   RPOB_MACCJ              Reviewed;        1180 AA.
AC   B9E8Q5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=MCCL_1866;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH18573.1; -; Genomic_DNA.
DR   RefSeq; WP_015912365.1; NC_011999.1.
DR   AlphaFoldDB; B9E8Q5; -.
DR   SMR; B9E8Q5; -.
DR   STRING; 458233.MCCL_1866; -.
DR   EnsemblBacteria; BAH18573; BAH18573; MCCL_1866.
DR   KEGG; mcl:MCCL_1866; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000001383; 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..1180
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000165811"
SQ   SEQUENCE   1180 AA;  132348 MW;  0FFD47B3983678A1 CRC64;
     MTGQLIQYGR HRKRRSYARI SEILELPNLI EIQTKSYDWF LKEGLIEMFK DISPIEDFTG
     NLSLEFVDYK LGEPKYDLDE SKNRDATYAA PLRVKVRLII KETGEVKEQE VFMGDFPLMT
     DTGTFVINGA ERVIVSQLVR SPSVYFNDKV DKNGKVSFGA TVIPNRGAWL EYETDAKDVV
     FVRIDRTRKL PITVLLRALG FSTDQEIIDL LGDNEYLRNA LDKDNTESTE AALLEIYERL
     RPGEPPTVEN AKSLLYSRFF DPKRYDLASV GRYKMNKKLH LKHRLFNQVL AEPIVNTETG
     EIVAEEGTLL DRRNLDQIID VLESNANQKV YDLDNGLLDE PIEIQSVKVY VPGDEEKRTT
     TIIGNAFPDD EVKCITPADI LSSVSYFFNL LAGVGFTDDI DHLGNRRLRS VGELLQNQFR
     IGLSRMERVV RERMSLQDTE SVTPQQLINI RPVIASIKEF FGSSQLSQFM DQANPLAELT
     HKRRLSALGP GGLTRERAGM EVRDVHYSHY GRMCPIETPE GPNIGLINSL SSYARVNEFG
     FIETPYRKVD IETNTVTSQI DYLTADEEDA YVVAQANARL DDNGKFLDDE VVCRFRGDNT
     VMARERMDYM DVSPKQVVSA ATACIPFLEN DDSNRALMGA NMQRQAVPLM NPEAPFVGTG
     MEHVAARDSG AAVVAKYKGR VEHVEARQIK VRRIVEEGGK EIETDLDVYK LAKFARSNSG
     TCYNQRPIVE AGNIVTKGEI LADGPSMELG EMALGRNVVV GFMTWDGYNY EDAVIMSERL
     VKDDVYTSIH IEEYESEARD TKLGPEEITR DIPNVSDNAL KNLDDRGIIF VGAEVRDGDI
     LVGKVTPKGV TELTAEERLL HAIFGEKARE VRDTSLRVPH GADGIVLDVK VFNREDGDEL
     PPGVNQLVRV YIVQKRKIHV GDKMCGRHGN KGVISRILPE EDMPFMPDGT PIDIMLNPLG
     VPSRMNIGQV LELHLGMAAK NLGLHVASPV FDGANDEDVW STIEEAGMAR DGKTVLYDGR
     TGEPFDNRVS VGVMYMLKLA HMVDDKLHAR STGPYSLVTQ QPLGGKAQFG GQRFGEMEVW
     ALEAYGAAYT LQEILTYKSD DTVGRVKTYE AIVKGENIPR PGVPESFRVL MKELQSLGLD
     VKVMDNKDEE IEMRDLEDDD FVDSKINIAK APMPEAEITE