RPOB_MYCPU
ID RPOB_MYCPU Reviewed; 1216 AA.
AC Q98Q23;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=MYPU_5460;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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; AL445565; CAC13719.1; -; Genomic_DNA.
DR PIR; B90580; B90580.
DR RefSeq; WP_010925347.1; NC_002771.1.
DR AlphaFoldDB; Q98Q23; -.
DR SMR; Q98Q23; -.
DR STRING; 272635.MYPU_5460; -.
DR EnsemblBacteria; CAC13719; CAC13719; CAC13719.
DR KEGG; mpu:MYPU_5460; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_14; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; MPUL272635:G1GT6-554-MON; -.
DR Proteomes; UP000000528; 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; 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; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1216
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047924"
FT REGION 1185..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 136663 MW; D2FA276E875D4F99 CRC64;
MPQKINYELK NFGQYTKRRD YSKTRFSLPL TDVLAIQKES FDWFLNKAIE ATLRKYYPIK
SSNNKVEIKY VLGSKRIEKP LVTEQKAVKE AKQKGISYSA RLYVKLQKHI TETGEISFDE
VILCDIPLMT SSGSFIINGF EKVIVSQLIR SPGAYFAQKT RDKQSDDLFN KVEVLPRIGS
WIEIKHKVTS NLDSVKIKID KHKSFLLTTF LSSFGFTEES MYKLFGNSET LKNTLSKDKI
LGKNKDIVEI RKEAQENIFR IVRRGDRITK EASQNLISNL LFNEKRYNLS KTGRYMLNRK
LSLFDRIITT YLAQDIVLKN VDPTMEAKIL YPKGTYITND IAIEIQNAFK EGLIKNIDLK
DYGITSDVYG KLLDTNPKLK NRMNIIGIYI FKSKKAMEKD GEKHFVIGND PTSVENHLLI
SDIVAIINYY FNLNENIGRD DDPDSLINKR IVSVGELLLN QLNIGLLKME KNTREKMSSK
EISRITPKNI TNNKMIQNQI KTFFNSSKLS QFMDQTNPLS EISTKRKITS LGPGGLNRDT
AQFEVRDVHA THYGRICPIE TPEGPNIGLI LNLATYAKVD EYGFLQTPYF KVTNGIVDFS
QPVYLTAHEE INRTFAQSSI SIDENGKITD EQVIVKSNFD YNVVSPKEVD YIDVSSKQMT
SLAASSIPFL ENNDANRALM GSNMQRQAVP LLFAEAPLVA TGIEADIAKF SPNNLKSTVD
GEVVFVDGSQ IKIKDSASEK GSIKTYQLKT FEKTNQGTVI SQSPIVKMGD KVLKGDLISD
SSSFKDGEMA LGKNVLVGFS TWNGYNYEDA IIVSERLVKD DVFTSIHIEE QTIQFRKSKA
GDDKLTADIP NASLKSRRHL DENGIVRIGS EVVTGDILVG RVSPKGDENI SPAEKLLNGI
FNQKISNEKD TSLKVKNGHQ GTVIDVEILS RENGNVLEEE IDMMIKVYVA QKRKIKVGDK
MAGRHGNKGV ISRVLPVEDM PYLEDGTPLD IILNPQGVPS RMNIGQVLEL HLGMAAKKLG
VKFVSPVFDG VKKADIMDAL EEAKLPRTGK MKVFDPTTGE KIDNEISVGV MYMFKLSHMV
DDKMHSRSIG PYSLITQQPL GGKSQNGGQR FGEMETWALE SYGAANILQE ILTYKSDDIQ
GRNNLYSALT SGTKLPKPGV PESFSVLAYE LRGLGIKLQI HEKEEEKQEL PSQEYESLNL
DQELKTASEN VSESEF
