RPOB_STAHJ
ID RPOB_STAHJ Reviewed; 1183 AA.
AC Q4L3K3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=SH2465;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05774.1; -; Genomic_DNA.
DR RefSeq; WP_011276718.1; NC_007168.1.
DR AlphaFoldDB; Q4L3K3; -.
DR SMR; Q4L3K3; -.
DR STRING; 279808.SH2465; -.
DR PRIDE; Q4L3K3; -.
DR EnsemblBacteria; BAE05774; BAE05774; SH2465.
DR KEGG; sha:SH2465; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000543; 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; 1.
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_0000047967"
FT REGION 1149..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; 133268 MW; F81D69A2ED8955C1 CRC64;
MAGQVVQYGR HRKRRNYARI SEVLELPNLI EIQTKSYDWF LKEGLLEMFR DISPIEDFTG
NLSLEFVDYR LGEPKYDLEE SKNRDATYAA PLRVKVRLII KETGEVKEQE VFMGDFPLMT
DTGTFVINGA ERVIVSQLVR SPSVYFNEKI DKNGRENYDA TIIPNRGAWL EYETDAKDVV
YVRIDRTRKL PLTVLLRALG FSNDQEIIDL LGDSEYLRNT LEKDGTENTE QALLEIYERL
RPGEPPTVEN AKSLLYSRFF DPKRYDLASV GRYKANKKLH LKHRLFNQRL AEPIVNSETG
EIVAEEGTVL DRRKLDEIME VLETNANSEV FELEGTVIDE PVEIQSIKVY VPNDEEGRTT
TVIGNALPDS EVKCITPADI IASMSYFFNL 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 NTEAPFVGTG
MEHVAARDSG AAITAKYRGR VEHVESKEIL VRRLVEENGT EHEGELDRYP LAKFKRSNTG
TCYNQRPIVS VGDVVEYNEI LADGPSMELG EMALGRNVVV GFMTWDGYNY EDAVIMSERL
VKDDVYTSIH IEEYESEARD TKLGPEEITR DIPNVSENAL 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 EAIVKGENIS RPSVPESFRV LMKELQSLGL
DVKVMDEQDN EIEMADVDDE DATERKVDLQ QKDVPETQKE TTD
