RPOB_MALP2
ID RPOB_MALP2 Reviewed; 1375 AA.
AC Q8EWX1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=MYPE790;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC43869.1; -; Genomic_DNA.
DR RefSeq; WP_011076905.1; NC_004432.1.
DR AlphaFoldDB; Q8EWX1; -.
DR SMR; Q8EWX1; -.
DR STRING; 272633.26453537; -.
DR EnsemblBacteria; BAC43869; BAC43869; BAC43869.
DR KEGG; mpe:MYPE790; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_14; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002522; 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; -; 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; 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..1375
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047921"
SQ SEQUENCE 1375 AA; 154733 MW; 9541C9BC279CFA27 CRC64;
MSKKKFIDKE ISKYVLRRDY SKIEKNFNEP NLLNLQKNAF HKFIDTELEG TIKSIFPIKS
IGGRYSLEYI GMKLEKPKRS EKEARNEGKT YDRPLYVDLA IVDNESGEVK KTTKSSKNKA
SNTDGIFFAS IPMITEKGTF IVNGIEKFVI SQIVRSPGAY ILTKSQIKLS NSRKRIQEGY
ICEILPAKGT LFFIFMAENK DFIQVMFRDA IGESTHTIPI TAFLKALGLN KEEILNIFAN
HKSIKNSLDN EIYNEKDVFE TDELINLRKN LNSSDSNRSY GVDTKLRELF KKYSSLKSQL
EAEGKNAEKQ KELNEVINNI ISEKAAKDLV INLSISTKNI DSKFRLSNKE TTYQSIIYNH
FFSNKSFDLS KAGRFKMARK MRLSERLYQR VLAEDLKDIN GKVVIKKNTL IQKHELDTIK
QLTKEGKLGI VHNVNLDERI SKMANVVKYE KINVYQDNDS QDEFIPIIGT DTSLDKPTLS
ISDILSITSY VINLDYDIGF YDDIDHLGNK RLKLIDELLK TRAQAGLVRI EKFINDKLAI
ADGANKSQEQ SEEQEPKKSL TVKSIINTKP FQISFKEFFN SHQLTQFLDQ QNPLAELTNK
RRISAMGPGG ISREDPNLDI RDVHYSHYGK ICPIETPEGM NIGLIMSLAT YASTDENGFL
ITPYRIVKNG VITDEIRWLT ALSEDEYIIA CSNLNVEKNK FKEDKVLCRY RSSWEFFDVK
DVDFIDISPK QVVSIAASSI PFLENDDANR ALMGANMQRQ ATPLISPIAP IVGTGNEYKI
AHDSGMAAVY DGEKDGTVSY VDGGTIKIKS GSEEKVYELT KFNKSNQNTC NNQVPIVSVG
EKVTKGTTIA DGPAMSNGEL ALGQNVLVAF TTWSGYNYED AIILSKRLFM EDIFTSIHIV
EYSVDCLKTK NGDEEITRDI PNVSESSKKY LDDEGIIMVG AEVKEGDVLV GKISPKGQVE
LTSEEKLLQA IFGDKSKNHK ETSLKVPHGG EGTVAMVKRF KVEDDYELNA DVIEQIKVYV
VQKRKIQIGD KMAGRHGNKG IISKIVPVED MPHLEDGTTI DIMLNPLGVP SRMNIGQILE
LHLGLAMKKL TLSKVLELYY DKKPASDFSL WFGIHEEASR NLIKNLEKIL NEKQIKSLDQ
ANKEFTDFDL SLALSRSGIS REKLIYKTAT PVFEGVNRTD LKEAMTEAGI DPINGKLGEG
KSGKFNLIDG RTGEYFDGEV SVGIMYMLKL DHMVDDKIHS RAVGPYSKIT QQPLGGKSQN
GGQRFGEMEV WALEAYGAAH NLRELLTIKS DDVKGRNNTY NAIIKGKPIP ESGLPESFKL
LTKQLQGLGL QVSITKELGK ANNNNFKDIN EYISNITNNA IKNDEDQQII EEMDI
