RPOB_LATSS
ID RPOB_LATSS Reviewed; 1197 AA.
AC Q38UQ2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=LCA_1775;
OS Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS subsp. sakei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=314315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23K;
RX PubMed=16273110; DOI=10.1038/nbt1160;
RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA Zagorec M.;
RT "The complete genome sequence of the meat-borne lactic acid bacterium
RT Lactobacillus sakei 23K.";
RL Nat. Biotechnol. 23:1527-1533(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; CR936503; CAI56083.1; -; Genomic_DNA.
DR RefSeq; WP_011375457.1; NC_007576.1.
DR AlphaFoldDB; Q38UQ2; -.
DR SMR; Q38UQ2; -.
DR STRING; 314315.LCA_1775; -.
DR PRIDE; Q38UQ2; -.
DR EnsemblBacteria; CAI56083; CAI56083; LCA_1775.
DR KEGG; lsa:LCA_1775; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; LSAK314315:LCA_RS08825-MON; -.
DR Proteomes; UP000002707; 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; 2.30.150.10; -; 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; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
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..1197
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224066"
FT REGION 1172..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1197 AA; 133762 MW; CC2D78E06E3E36BF CRC64;
MAGHLVNYGK HRTRRSYARI KEVLELPNLI EIQSNSYQWF LDEGLREMFD DIMPIDDFAG
NLSLEFVDYQ LLEPKYTVEE ARQHDANYSA PLHVTLKLTN HETGEIKSQD VFFGDFPLMT
DQGTFIINGA ERVIVSQLVR SPGVYFNSAI DKNSRTTYGT TVIPNRGAWL EFETDAKDIA
YVRIDRTRKI PMSVLVRALG YGSDQEIIDI LGDNDSLMLT LEKDIHKNTD DSRTEEALKD
VYERLRPGEP KTADSSRSLL FARFFDAKRY DLASVGRYKI NKKLSLKTRL LGQTLAETLA
DPDTGEVIAA KDTVVDRQVM DALAPYLDCE DFKAVTYQPS DEGVLPEPMT LQVIKVYSQK
TPDKEINLIG NGHIDAKVKH VIPADIIASM NYFFNLQEGL GSTDDIDHLG NRRIRSVGEL
LQNQFRIGLS RMERVVRERM SIQDTSTVTP QQLINIRPVV ASIKEFFGSS QLSQFMDQTN
PLGELTHKRR LSALGPGGLT RDRAGYEVRD VHYTHYGRMC PIETPEGPNI GLINSLASYA
VVNRYGFIET PYRRVSWDTH DVTDKIDYLT ADEEDNYVIA QANSPLNDDG SFVDNTVLAR
YKDDNIETSI DKLDYMDVSP KQVVAVATAC IPFLENDDSN RALMGANMQR QAVPLVNPHA
PLVGTGMEYK AAHDSGIALL AQHAGTVEYV DAKVIRVRRE DSSLDTYELM KFRRSNAGKN
YNQRPIVAKG DHVDVDEIIA DGPAMEKGEL ALGQNPLIAF MTWNMYNYED AIVLSERLVK
EDLYTSIHIE EYESEARDTK LGPEEITREI PNVGEDSLKD LDEFGIVRVG AEVKDGDILV
GKVTPKGVTE LSAEERLLHA IFGEKAREVR DTSLKVPHGG GGIIQDVKIF TREAGDELSP
GVNMMVRVYI TQKRKIQVGD KMAGRHGNKG TVSIVVPEED MPYTPDGTPV DILLSPMGVP
SRMNIGQVLE LHLGMAARNL GIHVATPVFD GAQDKDLWDA VREANMPSDG KSILYDGRTG
EPFDTRVSVG VMYYMKLAHM VDDKLHARSI GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL
EAYGAAYTLQ EILTYKSDDV VGRVKTYEAI VKGEPIPKPG VPESFRVLVK ELQSLGLDMK
VLDIDNQEIE LRDMDDDDDD VVNVDALSKY AKEQEEKKAQ QEAEKAQAAS AEDPSAE
