RPOB_RICTY
ID RPOB_RICTY Reviewed; 1374 AA.
AC P77941; Q68XM8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 127.
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=RT0129;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9661032; DOI=10.1128/aac.42.7.1845;
RA Troyer J.M., Radulovic S., Andersson S.G.E., Azad A.F.;
RT "Detection of point mutations in rpoB gene of rifampin-resistant Rickettsia
RT typhi.";
RL Antimicrob. Agents Chemother. 42:1845-1846(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1368.
RC STRAIN=ATCC VR-144 / Wilmington;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88811.1; Type=Miscellaneous discrepancy; Note=Sequence differs from that shown in the region 864-1035.; Evidence={ECO:0000305};
CC Sequence=AAB88812.1; Type=Miscellaneous discrepancy; Note=Sequence differs from that shown in the region 864-1035.; Evidence={ECO:0000305};
CC Sequence=AAD52032.1; Type=Miscellaneous discrepancy; Note=Sequence differs from that shown in the region 864-1035.; Evidence={ECO:0000305};
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DR EMBL; AF035659; AAB88811.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF035660; AAB88812.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE017197; AAU03614.1; -; Genomic_DNA.
DR EMBL; AF083622; AAD52032.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; WP_011190601.1; NC_006142.1.
DR AlphaFoldDB; P77941; -.
DR SMR; P77941; -.
DR STRING; 257363.RT0129; -.
DR EnsemblBacteria; AAU03614; AAU03614; RT0129.
DR KEGG; rty:RT0129; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000604; 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; -; 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 DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..1374
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047951"
FT CONFLICT 201
FT /note="F -> L (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="V -> I (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="T -> A (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1265
FT /note="H -> P (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1290
FT /note="G -> S (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1374 AA; 154647 MW; 0A4F14CE4354A319 CRC64;
MVSLRDNIES QPLSHNRRVR KNFGHINLVA DIPNLIEIQK NSYERNFLQL NIKDSERKNK
GLQSILNSIF PISDSSNIAN LEFVKYEFDT PKYDVDECSQ RSLSYAAPLK VTLRLSIWDI
DEDTGTREIK GIKEQEVYMG DIPLMTKNGT FIINGTERVV VSQMHRSPGV FFYHDEGKVH
SSGKLLYSAR VIPYRGSWLD FEFDAKDVIY FRIDRKRKLY ATTLLRAIGM NTEEIMKFYY
NSVTYKCIKN KGWSVKFIPQ HITAHRLTSD LVDADTGNVL LKAGQKITPR LAQKYFSIGL
NNILVTHETL IGKYLSEDLR DPESDEILAK IGEMITADML QVINDLKIKN VNVLVINPQS
GPYIRNTLFA DKNQDRETAL CDIFRVLRPG EPANIEAAES LFYNLFFDAE RYDLSEVGRI
KMNSRLELNI SEEITVLTID DIKNIVRILV ELKDGKGIID DIDHLGNRRV RSVGELIENQ
FRIGLVRIEK SVIERMSAGD VDTVMPHDLV NSKILVSVVK EFFSTSQLSQ FMDQTNPLSE
ITHKRRLSAL GPGGLSRDRA GFEVRDVHPT HYGRICPIET PEGQNIGLIN SMATYARINK
HGFIESPYRR VKDGYVTDEV VYLSAIEEGK YKIGQANSKV DQDGKLQGEF INCRVEGGNF
VMVEPYEVDF 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 IISGPKQITA GQTITTEMLK
GLSKGQLWQL IVEDANVMNE IEQIKIHYDE KKHALDKRFA TKVEKLQSGD DLPQGALKVV
KVFIATKHKL QPGDKMAGRH GNKGVISRIV PEEDMPFLED GTVVDIVLNP LGLPSRMNIG
QILETHLGWA SINLAKKIST LVKEYKDNNI DIEQIKKFLL ELYGKDINYI LEGSEEGIIS
FCNKVSKGVY FATPVFDGAK VQDVKDMLKL ADQDLSGQVK LIDGRTGEYF DRLVTVGHKY
LLKLHHLVDN KIHSRSIGPY SLVTQQPLGG KSHFGGQRFG EMECWALQAY GAAYTLQEML
TVKSDDVNGR IKTYDSIVRG ENNFESGIPE SFNVMIKEFR SLCLNVKLEV TASK
