RPOB_MYCCT
ID RPOB_MYCCT Reviewed; 1287 AA.
AC Q2ST48;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=MCAP_0070;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000123; ABC01305.1; -; Genomic_DNA.
DR RefSeq; WP_011386970.1; NC_007633.1.
DR AlphaFoldDB; Q2ST48; -.
DR SMR; Q2ST48; -.
DR PRIDE; Q2ST48; -.
DR EnsemblBacteria; ABC01305; ABC01305; MCAP_0070.
DR GeneID; 23778975; -.
DR KEGG; mcp:MCAP_0070; -.
DR HOGENOM; CLU_000524_4_1_14; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR PhylomeDB; Q2ST48; -.
DR Proteomes; UP000001928; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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; Transcription;
KW Transferase.
FT CHAIN 1..1287
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237305"
SQ SEQUENCE 1287 AA; 144569 MW; 22ED83665EB3FEA4 CRC64;
MAYKIRKINR NVERRDYTKV SMNLSLPNLI GIQTETFEWF KTKGIQEVLD EFFPILSFDG
SSVLTLENWG FKEPRLSVRQ AREESKIYDA PIYANLKLSV NKTEEIQKEF DGVDQEDTLK
VLTHWLEEKT GNGNITFKQQ SQNSYFFEIT IKKSEKPDLI QIDIIEDKKT SLICNVSIYK
SGEVFLGDFP LMTEAGTFII NGSQKVIVSQ LVRSPGAYFN KELNRKTGEM IYFADIIPSR
GTWLEYETDS KKIGSDAINP LYVKIDKSRK TTATSLLLAF GISKDDILNI FDNDEVLVET
LQQDSIIGDF KIDWSNQVQE IYKKIRQGET ATSEGASKFI NSILFDKRKY DLTKAGRFKL
KQKLSIKNRI LNKVIAEDIL DANNNVLIAK DTEVTKNNIQ EISKILDQDV MSIDLKYLSD
IPGNRKVQKI RVYKDSELKT DTTCLIGLTN SSNEEFITVA DILSTVSYLL NLKYNIGEID
DIDNLGNRRV RTVGELLQNQ FRMGLNRIDK NVKEKLATSD LYKVKTSTII NAKPLTAIIG
EFFNLSQLSQ FMDQINPLSE LTNKRRLTAL GPGGLSRDRA GLEVRDVHPS HYGRICPIET
PEGPNIGLIN NLSTYARVNE YGFITTPYRK VINGIIQNDQ VEYLTADQEK NFIIAQSNVN
QDENGKILDE IIVSRFNGDD YMAKVEEIHY IDVSPKQIVS VATSGIPFLE NDDANRALMG
ANMQRQAVPL IKPESPIVAT GIEFEAARDS GEAIVAKEDA IVKYVDSKTI ITDGESGIRT
YILSDYERSN NGTSLTQSPI VKVGDVVKKG EIIADGPSMD QGELAIGQNV VVAFSTYNGY
NFEDAIVMSE RIVIDDRFTS IHIDEYTLEV RNTKQGQEEV TREIPNMSEQ AKRHLDAEGI
VAIGTEVKVG DVLVGKVTPK GQVQLSPEDK LLHAIFGEKS RNVKDNSLRV PNGGEGIVQS
IKRFKAKSAL NPDGIELPAD IIEVIKVYVV QKRKIQEGDK MSGRHGNKGI ISRILPIEDM
PHLEDGTPVD IILNPQGVPS RMNIGQILEI HLGMAAKKLN QKVITPVFEG LNEKELEEIM
AEAGMTNYGK VTLIDGQTGE PFDKPIAVGV MYMLKLSHMV DDKIHARNVG PYSLITQQPL
GGKAQNGGQR FGEMEVWALE AYGAAHTLRE ILTIKSDDIK GRSKTYEAIV RSKRIPEPGI
PESFNVLSKE IMGLGFNMYM IDETGEKSAI NAYDKKDFEI DNYDDEILIK TDNLYIDDQD
VDAEFEDLTY VDENDILNSF ELDNEEE
