RPOB_UREP2
ID RPOB_UREP2 Reviewed; 1434 AA.
AC B1AIH5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=UPA3_0194;
OS Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=505682;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA Methe B.A., Glass J., Waites K., Shrivastava S.;
RT "Genome sequence of Ureaplasma parvum serovar 3.";
RL Submitted (FEB-2008) 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; CP000942; ACA32784.1; -; Genomic_DNA.
DR RefSeq; WP_006688964.1; NC_010503.1.
DR AlphaFoldDB; B1AIH5; -.
DR SMR; B1AIH5; -.
DR PRIDE; B1AIH5; -.
DR EnsemblBacteria; ACA32784; ACA32784; UPA3_0194.
DR GeneID; 29672197; -.
DR KEGG; upa:UPA3_0194; -.
DR HOGENOM; CLU_000524_4_3_14; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002162; 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; 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 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 PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..1434
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000086388"
SQ SEQUENCE 1434 AA; 162099 MW; FA407E25EC192F8B CRC64;
MQNNKNYTEK FITDKVMRRD YSKIKSNFEG PNLLEIQVES FKRFMEKDLK EVISSIFPLK
SPQGKYTLAF KGLKIKQPTK DESACRDEGK TFETPIYIDL ELTDNYTGEV KRAQRNTKTG
EDGIYLGAIP KMTEKGTFVI NGIEKFVISQ IVRSPGIYVL GKSSIKLNGS RKRLFEGKIC
EIYPSKGTLM LGYIPKDRHN IQIVARDSSG DNAQTFSVTT LLKAFGLTSA EILKIFNNEK
EIRESLEIEK YAPEYIFENS QENEIIFKIY SDAHDIHEKA DRRESNNKLK EEYIEQGSPL
LSKLKQLIFN YVEKNDEIDA LLHENKDVED ASFIKNNKKL YDEREEIINC IISEKAAKDI
VELLGINIKN IETLRHLGKA SYQIALQQHF FNKRLYDISS AGRYKFEKKL LLSERLYQKV
IANDIIDKKN NILIPKDTLI TKEHIELIKK ESRDKNIKWT KKINLLPTAL ESEIEQFLEY
ESIAVYKDND LRDETTEIVG LASGCKLQTL TVADLVATTS YIYNLNYEIG EFDDIDHLGN
KRLKLIHELL RARIATSMAR IEKFINEKLA ISDGSSNNIT NVNDKGIDTE LDREIEESDM
SDEEKKKAIS VKSIINTKQF QSLVKDFFNS HQLIQFIDQQ NPLAELTNKR RISAMGPGGI
SREDPNLDIR DVHHSHYSRI CPIETPEGMN IGLIMSLASL AKVDENGFIV APYYVVEDGV
VKEDYKYLTA HEDDNYIIAE SSVQLDENKR ILDEQVVARY RGSTGLFSPN EVDFIDIVPK
QVVSIAASAI PFIENDDGAR ALMGSNMQRQ ATPLIKPYAP IVGTGTEFKI AHDSGMAVVA
KNDGVVEFVD SQKIIIRNDN DKLDDYKLIK YRKSNQDTCN NQIPIVKVGQ RVHKSETIGD
GPAMQNGELA LGRNILVGYT TWRGYNFEDA IIISERLVDQ DVFTSIHIDE HTIQCMKTKN
GDEEITRDMP NVSDTAKRFL DNQGIVLVGA EVHEGDVLVG KTTPRGNVET APEDRLLQTI
FGDKSKTVKD SSLKVKHGQE GIVAAVKRIK SSDENGSELP DDVIEIIKVY IVQKRKIQVG
DKMAGRHGNK GIVSKVVPIQ DMPFLKDGTP LDIMLNPLGV PSRMNIGQIL ELHLGYAAAE
IGKKQLIQIA IDQLGYEKYI SLFGINEIIA KKLYENISNL IKHKQAKQAK DIDLIDVTII
LKELGLSYDD IGIKISTPVF DGANHDDIVS IMNEANIDIE NNKGKQVLYD GRTGEPFDGL
ISVGLTYMLK LDHMVDDKIH SRSVGPYSKI TQQPLGGKSQ NGGQRFGEME VWALEAYGAA
YNLLEILTIK SDDVQGRNQA YNAIIKGHDV VADGMPESFK LLTKQMQGLG LCITVETKDD
RMVDINEYTL NQNRLNNDDD EVILDENLKE INDSNEEIFN TNFNNNDYDD EENF
