RPOB_STAS1
ID RPOB_STAS1 Reviewed; 1183 AA.
AC Q49V52;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=SSP2213;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE19358.1; -; Genomic_DNA.
DR RefSeq; WP_011303839.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49V52; -.
DR SMR; Q49V52; -.
DR STRING; 342451.SSP2213; -.
DR EnsemblBacteria; BAE19358; BAE19358; SSP2213.
DR KEGG; ssp:SSP2213; -.
DR PATRIC; fig|342451.11.peg.2204; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000006371; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1183
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047968"
FT REGION 1153..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1183 AA; 132904 MW; 2796C3F391BF3A36 CRC64;
MAGQFVQYGR HRKRRNYARI SEVLELPNLI EIQTKSYDWF LEEGLLEMFR DISPIEDFTG
NLSLEFVDYR LGEPKYDLEE SKNRDTTYSA PLRVKVRLII KETGEVKEQE VFMGDFPLMT
DTGTFVINGA ERVIVSQLVR SPSVYFNEKL DKNGRTNFDA TIIPNRGAWL EYETDAKDVV
YVRIDRTRKL PLTVLLRALG FSTDQEIVDL LGDNEYLRNT LEKDGTETTD QALLEIYERL
RPGEPPTVEN AKSLLYSRFF DPKRYDLASV GRYKANKKLH LKHRLFNQKL AEPIVNTETG
EIVAEEGTVL DRRNLDEIMD VLEANANSEV FELEGTVIDE PVEIQSIKVY VPNDEEGRTT
TVIGNAFPDS EVKCITPADI IASMSYFFNL LSGIGFTDDI DHLGNRRLRS VGELLQNQFR
IGLSRMERVV RERMSIQDTD SVTPQQLINI RPVIASIKEF FGSSQLSQFM DQANPLAELT
HKRRLSALGP GGLTRERAQM EVRDVHYSHY GRMCPIETPE GPNIGLINSL SSYARVNEFG
FIETPYRKVD LETNSITDQI DYLTADEEDS YVVAQANSTL DENGRFIADE VVCRFRGNNT
VMAKEKMDYM DVSPKQVVSA ATACIPFLEN DDSNRALMGA NMQRQAVPLM NPESPFVGTG
MEHVAARDSG AAIVAKRKGR VEHVESNEIL VRQLIEEDGQ EYEGELDRYP LAKFKRSNTG
TCYNQRPIVA SGDVVTKGEI LADGPSMELG EMALGRNVVV GFMTWDGYNY EDAVIMSERL
VKDDVYTSIH IEEYESEARD TKLGPEEITR DIPNVSDSAL KNLDDRGIVY VGAEVNDGDI
LVGKVTPKGV TELTAEERLL HAIFGEKARE VRDTSLRVPH GAGGIVLDVK VFNREEGDDT
LSPGVNQLVR VYIVQKRKIH VGDKMCGRHG NKGVISKLVP EEDMPYLPDG TPIDIMLNPL
GVPSRMNIGQ VLELHLGMAA KNLGIHVASP VFDGASDEDV WSTIEEAGMA RDGKTVLYDG
RTGEPFDNRI SVGVMYMLKL AHMVDDKLHA RSTGPYSLVT QQPLGGKAQF GGQRFGEMEV
WALEAYGAAY TLQEILTYKS DDTVGRVKTY ESIVKGENIT KPGVPESFRV LMKELQSLGL
DVKIMDEHDN EIDMQDNEEE DVVERKVDLQ QKDAPQSQKE VTD
