(data stored in SCRATCH3701 zone)

SWISSPROT: 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   11-DEC-2019, entry version 120.
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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
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};
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   SMR; P77941; -.
DR   STRING; 257363.RT0129; -.
DR   PRIDE; P77941; -.
DR   EnsemblBacteria; AAU03614; AAU03614; RT0129.
DR   KEGG; rty:RT0129; -.
DR   eggNOG; ENOG4108IIJ; Bacteria.
DR   eggNOG; COG0085; LUCA.
DR   HOGENOM; HOG000218612; -.
DR   KO; K03043; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   BioCyc; RTYP257363:G1G0L-135-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
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; -; 2.
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; 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;
DR   PRODOM; P77941.
DR   SWISS-2DPAGE; P77941.
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
//

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