RPOB_STRM5
ID RPOB_STRM5 Reviewed; 1384 AA.
AC B4SKV6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Smal_0749;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-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; CP001111; ACF50454.1; -; Genomic_DNA.
DR RefSeq; WP_004145255.1; NC_011071.1.
DR AlphaFoldDB; B4SKV6; -.
DR SMR; B4SKV6; -.
DR STRING; 391008.Smal_0749; -.
DR EnsemblBacteria; ACF50454; ACF50454; Smal_0749.
DR KEGG; smt:Smal_0749; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; SMAL391008:SMAL_RS03825-MON; -.
DR Proteomes; UP000001867; 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; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
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; 3.
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; Transcription;
KW Transferase.
FT CHAIN 1..1384
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165823"
SQ SEQUENCE 1384 AA; 154327 MW; 6C858268DD4ED421 CRC64;
MTSYSFTEKK RIRKDFGKQR SILEVPFLLA IQVDSYREFL QENVDPAKRT DHGLHAALKS
VFPIASYSGN AALEYVGYKL GEPVFDEREC RQRGMSYGAP LRVTVRLVIY DRESSTKAIK
YVKEQEVYLG EIPLMTENGT FIVNGTERVI VSQLHRSPGV FFDHDRGKTH SSGKLLYSAR
IIPYRGSWLD FEFDPKDALF TRIDRRRKLP VSILLRALGY SNEEMLAEFF EINTFHINPD
EGVQLELVPE RLRGETLGFD LADGDKVIVE AGKRITARHI KQLEASGIAA LAVPDDYIVG
RILSHDVVDA STGELLAQAN DEITDEQLQA FRKAGVDAVG TLWVNDLDRG PYLSNTLRID
PTKTQLEALV EIYRMMRPGE PPTKDAAQNL FHNLFFTFER YDLSAVGRMK FNRRVGRKET
TGEAVLYDRK YYGERNDEES KRLVAAHGDS SDILDVIKVL TEIRNGRGVV DDIDHLGNRR
VRSVGEMAEN VFRVGLVRVE RAVKERLSMA ESEGLTPQEL INAKPVAAAI KEFFGSSQLS
QFMDQNNPLS EVTHKRRVSA LGPGGLTRER AGFEVRDVHP THYGRVCTIE TPEGPNIGLI
NSLAVYARTN QYGFLETPYR KVVDGKVYDE VEFLSAIEEN EYVIAQANAL TNADSVLTEQ
FVPCRFQGES LLKPPAEVHF MDVSPMQTVS IAAALVPFLE HDDANRALMG ANMQRQAVPT
LRAQKPLVGT GIERAVARDS GVTVNARRGG EIVQIDAARI VVKVVEEEIV GATDAGVDIY
NLVKYTRSNQ NTCINQRPLV QVGDIIARGD VLADGPSTDI GELALGQNML IAFMPWNGYN
FEDSILLSER VVEEDRYTTI HIEELTCVAR DTKLGPEEIS ADIPNVSEQA LNRLDESGVV
YIGAEVRAGD IMVGKVTPKG ESQLTPEEKL LRAIFGEKAS DVKDSSLRVP PGMDGTVIDV
QVFTRDGIEK DKRARQIEES EIKRVKKDFD DQFRILEAAI YMRLRSQIVG KVVNGGAGLK
KGDVISDAFL DGLKKADWFA LRMKDEDASE AIERAQKQIQ AHEKEFERRF ADKRGKITAG
DDLAPGVLKM VKVFLAVKRR IQPGDKMAGR HGNKGVVSNV VPVEDMPYMA SGETVDIVLN
PLGVPSRMNI GQILEVHLGW AAKGLGRKIQ AMMEAQAAVA DLRKFLDDIY NHDDTNVANR
VDLSQFSDEE LLRLARNLTD GVPMATPVFD GATEAEIKRM LELADLPSSG QTQLYDGRTG
EAFDRHTTVG YMHYLKLNHL VDDKMHARST GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL
EAYGAAYTLQ EMLTVKSDDV QGRNQMYKNI VDGEHEMVAG MPESFNVLVK EIRSLAINME
LEDN
