RPOB_UREU1
ID RPOB_UREU1 Reviewed; 1434 AA.
AC B5ZAZ3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=UUR10_0178;
OS Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=565575;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33699 / Western;
RA Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL Submitted (OCT-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; CP001184; ACI59846.1; -; Genomic_DNA.
DR RefSeq; WP_004025875.1; NC_011374.1.
DR AlphaFoldDB; B5ZAZ3; -.
DR SMR; B5ZAZ3; -.
DR STRING; 565575.UUR10_0178; -.
DR EnsemblBacteria; ACI59846; ACI59846; UUR10_0178.
DR GeneID; 45015728; -.
DR KEGG; uue:UUR10_0178; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_14; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002018; 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_1000141747"
SQ SEQUENCE 1434 AA; 162186 MW; 0C0435F1021EFA19 CRC64;
MQNNKNYTEK FITDKVTRRD YSKIKSNFEG PNLLEIQVES FKRFMEKDLK EVISGIFPLK
SPQGKYTLAF KGLKIKQPTK DESACRDEGK TFETPIYIDL ELTDNYTGEV KRAQRNAKTG
EDGIYLGAIP KMTEKGTFVI NGIEKFVISQ IVRSPGIYVL GKSSIKLNGS RKRLFEGKIC
EIYPSKGTLM LGYIPKDRHN IQIVARDSSG DNAQTFSITT LLKAFGLTSA EILKIFNNEK
EIRESLEVEK YSPEYIFENS QENEIIFKIY SDAHDIHEKA DRRESNNKLR EEYIEQGSPL
LSKLKELIFD YVEKSDEIDA LLHENKDVED ANFIKNNKKL YDEREEIINC IISEKAAKDI
VELLGINIKN VETLRHLGKA SYQLALQQHF FNKRLYDISS AGRYKFEKKL LLSERLYQKV
IARDIIDKKN NILIPKDTLI TKEHIELIKK ESRDKNIKWT RKINLLPIAL ETEIEQFLEY
ESIAVYKDND LRDETTEIVG LAPGCKLQTL TVADLVATTS YIYNLNYEIG EFDDIDHLGN
KRLKLIHELL RARIATSMAR IEKFINEKLA ISDGSSNNIT NVNDKGIDTE LDREVEESDM
SDEEKKKAIS VKSIINTKQF QSLVKDFFNS HQLIQFIDQQ NPLAELTNKR RISAMGPGGI
SREDPNLDIR DVHHSHYSRI CPIETPEGMN IGLIMSLASL AKVDENGFIV APYYVVEDGV
VKEECKYLTA HEDDNYIIAE SSVQLDENKR ILDEQVVARY RGSTGLFSPH EVDFIDIVPK
QVVSIAASAI PFIENDDGAR ALMGSNMQRQ ATPLIKPYAP IVGTGTEFKI AHDSGMAVVA
KNDGVVEFVD SQKIVIKNDN DKLDEYKLIK YRKSNQDTCN NQIPIVKIGQ KVHKSETIGD
GPAMQNGELA LGRNILVGYT TWRGYNFEDA IIISERLVDQ DVFTSIHIDE HTIQCMKTKN
GDEEITRDMP NVSDTAKRFL DNQGIVLVGA EVHEGDVLVG KTTPRGNVET APEDRLLQTI
FGDKSKTVKD SSLKVKHGQE GIVAAVKRIK STDENGSELP DDVIEIIKVY IVQKRKIQVG
DKMAGRHGNK GIVSKVVPIQ DMPFLKDGTP LDIMLNPLGV PSRMNIGQIL ELHLGYAAAE
IGKKQLIQIA IDQLGYEKYI SLFGINEIIA KKLYEKITNL IKHKQAKQPK DIDLIDITIV
LKELGLSYDD IGIKISTPVF DGANHDDIVD IMNEANIDIE NNKGKQVLYD GRTGEAFDGL
ISVGLTYMLK LDHMVDDKIH SRSVGPYSKI TQQPLGGKSQ NGGQRFGEME VWALEAYGAA
YNLLEILTIK SDDVQGRNQA YNAIIKGHDV VADGMPESFK LLTKQMQGLG LCITVETKDD
RMIDINEYTL NQNRLNNDDD EVIFDESIKE INENNQQVFN TDFNDNDYDD EENF
