RPOB_RICPR
ID RPOB_RICPR Reviewed; 1374 AA.
AC O52271; Q9RH37;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=RP140;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9555894; DOI=10.1128/jb.180.8.2118-2124.1998;
RA Rachek L.I., Tucker A.M., Winkler H.H., Wood D.O.;
RT "Transformation of Rickettsia prowazekii to rifampin resistance.";
RL J. Bacteriol. 180:2118-2124(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC VR-142 / Breinl;
RX PubMed=10508014; DOI=10.1128/aac.43.10.2400;
RA Drancourt M., Raoult D.;
RT "Characterization of mutations in the rpoB gene in naturally rifampin-
RT resistant Rickettsia species.";
RL Antimicrob. Agents Chemother. 43:2400-2403(1999).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
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; AF034531; AAC38354.1; -; Genomic_DNA.
DR EMBL; AJ235270; CAA14608.1; -; Genomic_DNA.
DR EMBL; AF076437; AAF22439.1; -; Genomic_DNA.
DR PIR; A71724; A71724.
DR RefSeq; NP_220531.1; NC_000963.1.
DR RefSeq; WP_010886216.1; NC_000963.1.
DR AlphaFoldDB; O52271; -.
DR SMR; O52271; -.
DR STRING; 272947.RP140; -.
DR EnsemblBacteria; CAA14608; CAA14608; CAA14608.
DR GeneID; 57569268; -.
DR KEGG; rpr:RP140; -.
DR PATRIC; fig|272947.5.peg.142; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002480; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; -; 1.
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 Antibiotic resistance; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..1374
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047950"
FT VARIANT 10
FT /note="S -> A (in strain: Breinl)"
FT VARIANT 15
FT /note="H -> L (in strain: Breinl)"
FT VARIANT 19
FT /note="I -> L (in strain: Breinl)"
FT VARIANT 96
FT /note="D -> E (in strain: Breinl)"
FT VARIANT 195
FT /note="R -> I (in strain: Breinl)"
FT VARIANT 216
FT /note="K -> R (in strain: Breinl)"
FT VARIANT 256
FT /note="K -> E (in strain: Breinl)"
FT VARIANT 273
FT /note="D -> Y (in strain: Breinl)"
FT VARIANT 282
FT /note="K -> N (in strain: Breinl)"
FT VARIANT 299
FT /note="G -> S (in strain: Breinl)"
FT VARIANT 310
FT /note="L -> F (in strain: Breinl)"
FT VARIANT 546
FT /note="R -> K (in rifampicin resistant mutant)"
SQ SEQUENCE 1374 AA; 154583 MW; 384676DFF6584DB4 CRC64;
MVSLRDNIES QPLSHNRRIR KNFGHINLVA DIPNLIEIQK NSYEKNFLQL NIKDSERKNK
GLQSILNSIF PISDSSNIAN LEFVKYEFDT PKYDVDECSQ RSLSYAAPLK VTLRLSIWDI
DEDTGTREIK GIKEQEVYMG DIPLMTKNGT FIINGTERVV VSQMHRSPGV FFYHDEGKVH
SSGKLLYSAR VIPYRGSWLD FEFDAKDIIY FRIDRKRKLY ATTLLRAIGM STEEIIKFYY
NSVTYKFVKN KGWSVKFIPQ HITAHRLTSD LVDADTGNVL LKAGQKITPR LAQKYFGVGL
NNILVTHETL IGKYLSEDLR DPASDEVLAK IGEMITSDML KVINDLKIKN VNVLVINPQS
GSYIRNTLFA DKNQDREAAL CDIFRVLRPG EPANIEAAES LFYNLFFDAE RYDLSEVGRI
KMNSRLELNI SEEVTVLTID DIKNIVRILV ELKDGKGIID DIDHLGNRRV RSVGELIENQ
FRIGLVRMEK SVIERMSAGD VDTVMPHDLV NSKILVSVVK EFFSTSQLSQ FMDQTNPLSE
ITHKRRLSAL GPGGLSRDRA GFEVRDVHPT HYGRICPIET PEGQNIGLIN SMATYARINK
HGFIESPYRR VKNGYVTDEV VYLSAIEEGK YKIGQANSKV DQDGKLQGEF INCRVEGGNF
VMVEPDEVDF IDVTPMQVVS VAASLIPFLE NDDANRALMG SNMQRQAVPL IKTEAPFVGT
GVEGVVAKDS GASVLALHDG IVERVDSNRI VIRTLEQKVD GSPSVDIYNL LKFQKSNHNT
CINQKPLVKV GHYVKKNDII ADGPSTDNGE IALGRNVLVA FLPWNGYNFE DSILISERIV
KEDVFTSIHI EEFEVIARDT RLGPEEITRD IPNVSEEALR HLDEVGIIYV GAEVKAGDIL
VGKVTPKSES PITPEEKLLR AIFGEKAFDV KDSSLHVPSG VSGTVVEVRI FSRRGVEKDQ
RAIAIEKQQI EKLAKDRDDE LEIIEHFVFS WLEKLLVGHV IINGPKQITA GQTITTEMLK
GLSKGQLWQI TVEDANVMNE IEQIKIHYDE KKYALDKRFT TKVEKLQSGD DLPQGALKVV
KVFIATKHKL QPGDKMAGRH GNKGVISRIV PEEDMPFLED GTVVDIVLNP LGLPSRMNIG
QILETHLGWA SINLAKKIST LVKEYKDNHI DIEEIKKFLL ELYGKDINYI LEGSEEEIIS
FCNKVSKGVY FATPVFDGAK VQDVKDMLEL AGQDLSGQVK LIDGRTGEYF DRLVTVGHKY
LLKLHHLVDN KIHSRSIGPY SLVTQQPLGG KSHFGGQRFG EMECWALQAY GAAYTLQEML
TVKSDDVNGR IKTYDSIVRG ENNFESGIPE SFNVMIKEFR SLCLNVKLEV TPSK
