RPOB_STACT
ID RPOB_STACT Reviewed; 1183 AA.
AC B9DKV0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Sca_0199;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(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; AM295250; CAL27112.1; -; Genomic_DNA.
DR RefSeq; WP_012664227.1; NC_012121.1.
DR AlphaFoldDB; B9DKV0; -.
DR SMR; B9DKV0; -.
DR STRING; 396513.SCA_0199; -.
DR PRIDE; B9DKV0; -.
DR GeneID; 60546105; -.
DR KEGG; sca:SCA_0199; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; SCAR396513:SCA_RS01025-MON; -.
DR Proteomes; UP000000444; 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_1000165821"
FT REGION 1155..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1183 AA; 133212 MW; F1E29D4613A3A212 CRC64;
MAGKFVQYGR HRKRRNYARI SEVLELPNLI EIQTKSYDWF LKEGLLEMFR DISPIEDFTG
NLSLEFVDYR LGEPKYDLEE SKNRDATYAA PLRVKVRLIN KETGEVKDQE VFMGDFPLMT
DTGTFVINGA ERVIVSQLVR SPSVYFNEKI DKNGRENYDA TVIPNRGAWL EFETDAKDIV
YVRIDRTRKL PLTVLLRALG YSTDQSIIDL LGDNEYLRNT LEKDSTENTE QALLEIYERL
RPGEPPTVEN AKSLLYSRFF DPKRYDLASV GRYKMNKKLH LKHRLFNQKL AEPIVNSDTG
EIVAEEGTVL DRRKLDEIMD VLESNANIEV DELDDSIVNE PVEIQSIKVY VPNDEEGRTT
TVIGNAFPDS EVKCITPADI VASMSYFFNL LHGIGQTDDI DHLGNRRLRS VGELLQNQFR
IGLSRMERVV RERMSIQDTD SITPQQLINI RPVIASIKEF FGSSQLSQFM DQANPLAELT
HKRRLSALGP GGLTRERAQM EVRDVHYSHY GRMCPIETPE GPNIGLINSL SSYARVNEFG
FIETPYRKVD LETNTVTDQI DYLTADEEDS YVVAQANSRL DDEGHFISEE VVCRFRGNNT
MMDRDKMDYM DVSPKQVVSA ATACIPFLEN DDSNRALMGA NMQRQAVPLM NPESPFVGTG
MEHATARDSG AAVINKHFGR VEHVESNEIK VRRIIEEDGQ QYDGELDTYR LAKFKRSNSG
TCYNQRPIVK DGDIVSQGEI LADGPSMELG EMALGRNVVV GFMTWDGYNY EDAVIMSERL
VKDDVYTSIH IEEYESEARD TKLGPEEITR DIPNVAESAL KNLDERGIVY VGAEVKDGDI
LVGKVTPKGV TELTAEERLL HAIFGEKARE VRDTSLRVPH GAGGIVLDVK VFNREDGDDS
LSPGVNQLVR VYIVQKRKIH VGDKMCGRHG NKGVISKIVP EEDMPYLPDG TPIDIMLNPL
GVPSRMNIGQ VLELHLGMAA KNLGIHVASP VFDGANDDDV WSTIEEAGMA RDGKTVLYDG
RTGEPFDNRI SVGVMYMLKL AHMVDDKLHA RSTGPYSLVT QQPLGGKAQF GGQRFGEMEV
WALEAYGAAY TLQEILTYKS DDTVGRVKTY EAIVKGENIS KPSVPESFRV LMKELQSLGL
DVKVMDEDDK EIEMADVDED DVNEHKVNIQ QSSIPESQKE TTD
