RPOB_BACP2
ID RPOB_BACP2 Reviewed; 1196 AA.
AC A8F976;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-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=BPUM_0093;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(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; CP000813; ABV60793.1; -; Genomic_DNA.
DR AlphaFoldDB; A8F976; -.
DR SMR; A8F976; -.
DR STRING; 315750.BPUM_0093; -.
DR EnsemblBacteria; ABV60793; ABV60793; BPUM_0093.
DR KEGG; bpu:BPUM_0093; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001355; 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; 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..1196
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000329166"
FT REGION 1155..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1196 AA; 133964 MW; BBD516E9334353A4 CRC64;
MNQLTGQLVQ YGRHRQRRSY ARISEVLELP NLIEIQTSSY QWFLDEGLRE MFQDISPIED
FTGNLSLEFI DYSLGDPKYP VAESKERDVT YSAPLRVKVR LINKETGEVK DQDVFMGDFP
IMTDTGTFII NGAERVIVSQ LVRSPSVYFS GKVDKNGKKG FTATVIPNRG AWLEYETDAK
DVVYVRIDRT RKLPVTVLLR ALGFSSDQEI LDLIGENEYL RNTLEKDNTE NADKALLEIY
ERLRPGEPPT VENAKSLLDS RFFDPKRYDL ANVGRYKINK KLHIKNRLFN QKLAETLVDP
ETGEILAEKG QILDRRVLDK VLPYLENGIG FRKLYPNGGV VEDEVELQSI KIYAPSDQEG
EQVINVIGNA YVEEAVKNIT PSDIIASISY FFNLLHGVGD TDDIDHLGNR RLRSVGELLQ
NQFRIGLSRM ERVVRERMSI QDTNTITPQQ LINIRPVIAS IKEFFGSSQL SQFMDQTNPL
AELTHKRRLS ALGPGGLTRE RAGMEVRDVH YSHYGRMCPI ETPEGPNIGL INSLSSFAKV
NRFGFIETPY RRVDPETGKV TPRIDYLTAD EEDNYVVAQA NALLADDGSF IDDNIIARFR
GENTVVPRNR VDYMDVSPKQ VVSAATACIP FLENDDSNRA LMGANMQRQA VPLMQPESPI
VGTGMEYVSG KDSGAAVICR YPGVVERVEA KNIWVRRYED VDGQQVKGNL DKYSLLKFVR
SNQGTCYNQR PIVSVGDEVV KGEILADGPS MEKGELALGR NVMVGFMTWD GYNYEDAIIM
SERLVKDDVY TSIHIEEYES EARDTKLGPE EITRDIPNVG EDALRNLDER GIIRIGAEVK
DGDLLVGKVT PKGVTELTAE ERLLHAIFGE KAREVRDTSL RVPHGGGGII HDVKVFNRED
GDELPPGVNQ LVRVYIVQKR KISEGDKMAG RHGNKGVISK ILPEEDMPYL PDGTPIDIML
NPLGVPSRMN IGQVLELHMG MAARYLGIHI ASPVFDGARE EDVWETLEEA GMSRDAKTVL
YDGRTGEPFD NRVSVGIMYM IKLAHMVDDK LHARSTGPYS LVTQQPLGGK AQFGGQRFGE
MEVWALEAYG AAYTLQEILT VKSDDVVGRV KTYEAIVKGD NVPEPGVPES FKVLIKELQS
LGMDVKILSG DEEEIEMRDL EDDEETKKAD GLALSNDEDA ADLAPVDLER DAVTKE