RPOB_METPP
ID RPOB_METPP Reviewed; 1375 AA.
AC A2SLG5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Mpe_A3451;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM96404.1; -; Genomic_DNA.
DR RefSeq; WP_011831025.1; NC_008825.1.
DR AlphaFoldDB; A2SLG5; -.
DR SMR; A2SLG5; -.
DR STRING; 420662.Mpe_A3451; -.
DR PRIDE; A2SLG5; -.
DR EnsemblBacteria; ABM96404; ABM96404; Mpe_A3451.
DR KEGG; mpt:Mpe_A3451; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000366; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1375
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300346"
SQ SEQUENCE 1375 AA; 152767 MW; 758874096936E645 CRC64;
MAQATPYSYT ERKRIRKSFG KRENVLGVPY LLTMQKDSYV AFLQKDVPPQ KRKPEGLQAA
FLSAFPIVSH NGFVEMKYIE FNMAKPAFDT RECQQRGLTY AAAVRAKLQM IIYDRETSTS
QSKVVKEIKE QEVYMGEVPL MTDYGSFIVN GTERVIVSQL HRSPGVFFEH DKGKTHSSGK
LLFSARIIPY RGSWLDFEFD PKDILYFRVD RRRKMPVTIL LKAIGLNPEQ ILANFFVFDN
FRLMDSGAQM EFVADRLRGE IARFDLTDKA GAVIVEKDKR ITARHTRALE ASGTSFISVP
EDFLVGRVLA KNMVDADTGE IIAKANDELT DSLLKKLRTA GIKDIQCLYT NELDMGAYIS
QTLASDETAD ELAARVAIYR MMRPGEPPTE DAVQALFNRL FYSEDTYDLS RVGRMKFNAR
VGRDTAEGRM VLANDDILDV VKILVELRNG RGEVDDIDHL GNRRVRCVGE LAENQYRSGL
ARIEKAVKER LGQAETEALM PHDLINSKPI SAALKEFFGA SQLSQFMDQT NPLSEITHKR
RVSALGPGGL TRERAGFEVR DVHPTHYGRV CPIETPEGPN IGLINSLALY AQLNEYGFLE
TPYRRVIDSK VTDQIDYLSA IEEGKYVIAQ ANAGLDKDGK LIDELVSARE SGESVLTSPE
RIQYMDVAPT QIVSVAASLV PFLEHDDANR ALMGANMQRQ AVPVLRPEKA FVGTGVERVS
AVDSGTVVTA KRGGVVDYID TNRIVIRVND AETVAGEVGV DIYNLIKYQR SNQNTNIHQR
PIVQRGDQVG AGDVIADGAS TDIGELALGQ NMLVAFMPWN GYNFEDSILI SERVVADDRY
TSIHIEELVV MARDTKLGSE EITRDIPNLS EQQLGRLDES GIVYIGAEVN PGDVLVGKVT
PKGETTLTPE EKLLRAIFGE KASDVKDTSL RVDQGTNGTV IDVQVFTREG IQRDKRAQQI
IDDELKRFRL DLNDQLRIVE ADAFDRIEKL LAGKTANGGP NKLAKGTPID KAYLASVDKY
HWFDIRPADD DIANQLESIK NSLEQTRHSF DLAFEEKRKK LTQGDELPAG VLKMVKVYLA
VKRRLQPGDK MAGRHGNKGV VSKIVPVEDM PYMADGTPCD IVLNPLGVPS RMNVGQVLEV
HLGWAAKGIG QRIGDLLQQE AKIADVRKFL DELYNKSGGK SEGLNGLSDA EITEMATNLA
QGVPFATPVF DGATEEEIRA MMHLAYPDEI AAAKGLNATR TQATLHDGRT GDAFERPVTV
GYMHVLKLHH LVDDKMHARS TGPYSLVTQQ PLGGKAQFGG QRFGEMEVWA LEAYGASYVL
QEMLTVKSDD VNGRTKVYES IVKGEHAIEA GMPESFNVLV KEIRSLGIDI ELERN
