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RPOA_BACSU
ID   RPOA_BACSU              Reviewed;         314 AA.
AC   P20429;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            Short=RNAP subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059, ECO:0000269|PubMed:18289874};
DE   AltName: Full=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE   AltName: Full=Transcriptase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
GN   Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059}; OrderedLocusNames=BSU01430;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2496109; DOI=10.1128/jb.171.5.2553-2562.1989;
RA   Boylan S.A., Suh J.-W., Thomas S.M., Price C.W.;
RT   "Gene encoding the alpha core subunit of Bacillus subtilis RNA polymerase
RT   is cotranscribed with the genes for initiation factor 1 and ribosomal
RT   proteins B, S13, S11, and L17.";
RL   J. Bacteriol. 171:2553-2562(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8635744; DOI=10.1016/0378-1119(95)00757-1;
RA   Suh J.-W., Boylan S.A., Oh S.H., Price C.W.;
RT   "Genetic and transcriptional organization of the Bacillus subtilis spc-
RT   alpha region.";
RL   Gene 169:17-23(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
RX   PubMed=3093467; DOI=10.1128/jb.168.1.65-71.1986;
RA   Suh J.-W., Boylan S.A., Price C.W.;
RT   "Gene for the alpha subunit of Bacillus subtilis RNA polymerase maps in the
RT   ribosomal protein gene cluster.";
RL   J. Bacteriol. 168:65-71(1986).
RN   [5]
RP   SUBUNIT.
RC   STRAIN=168;
RX   PubMed=6802805; DOI=10.1128/jb.150.2.977-980.1982;
RA   Achberger E.C., Tahara M., Whiteley H.R.;
RT   "Interchangeability of delta subunits of RNA polymerase from different
RT   species of the genus Bacillus.";
RL   J. Bacteriol. 150:977-980(1982).
RN   [6]
RP   FUNCTION, AND SUBUNIT.
RC   STRAIN=BS200;
RX   PubMed=18289874; DOI=10.1016/j.pep.2008.01.006;
RA   Yang X., Lewis P.J.;
RT   "Overproduction and purification of recombinant Bacillus subtilis RNA
RT   polymerase.";
RL   Protein Expr. Purif. 59:86-93(2008).
RN   [7]
RP   SUBUNIT.
RC   STRAIN=168;
RX   PubMed=21710567; DOI=10.1002/pmic.201000790;
RA   Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA   Hecker M., Becher D., Polard P., Noirot P.;
RT   "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL   Proteomics 11:2992-3001(2011).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000269|PubMed:18289874}.
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_00059,
CC         ECO:0000269|PubMed:6802805};
CC   -!- SUBUNIT: Homodimer. RNAP is composed of a core of 2 alpha, a beta and a
CC       beta' subunit. The core is associated with a delta subunit, and at
CC       least one of epsilon or omega (PubMed:6802805, PubMed:18289874,
CC       PubMed:21710567). When a sigma factor is associated with the core the
CC       holoenzyme is formed, which can initiate transcription
CC       (PubMed:18289874). {ECO:0000255|HAMAP-Rule:MF_00059,
CC       ECO:0000269|PubMed:18289874, ECO:0000269|PubMed:21710567,
CC       ECO:0000269|PubMed:6802805}.
CC   -!- INTERACTION:
CC       P20429; P25144: ccpA; NbExp=5; IntAct=EBI-5247865, EBI-5247535;
CC       P20429; P39779: codY; NbExp=2; IntAct=EBI-5247865, EBI-7827914;
CC   -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC       transcription, whereas the C-terminal domain is involved in interaction
CC       with transcriptional regulators and with upstream promoter elements.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
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DR   EMBL; M26414; AAA22217.1; -; Genomic_DNA.
DR   EMBL; L47971; AAB06826.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11919.1; -; Genomic_DNA.
DR   EMBL; M13957; AAA22708.1; -; Genomic_DNA.
DR   PIR; E32307; E32307.
DR   RefSeq; NP_388024.1; NC_000964.3.
DR   RefSeq; WP_003225835.1; NZ_JNCM01000029.1.
DR   PDB; 1Z3E; X-ray; 1.50 A; B=245-314.
DR   PDB; 3GFK; X-ray; 2.30 A; B=240-314.
DR   PDB; 3IHQ; X-ray; 1.90 A; B=245-314.
DR   PDB; 6WVJ; EM; 3.36 A; A/B=1-314.
DR   PDB; 6WVK; EM; 3.36 A; A/B=1-314.
DR   PDB; 6ZCA; EM; 4.20 A; U/V=1-314.
DR   PDB; 6ZFB; EM; 3.90 A; U/V/u/v=1-314.
DR   PDB; 7CKQ; EM; 4.40 A; A/B=1-314.
DR   PDB; 7F75; EM; 4.20 A; A/B/I=1-314.
DR   PDBsum; 1Z3E; -.
DR   PDBsum; 3GFK; -.
DR   PDBsum; 3IHQ; -.
DR   PDBsum; 6WVJ; -.
DR   PDBsum; 6WVK; -.
DR   PDBsum; 6ZCA; -.
DR   PDBsum; 6ZFB; -.
DR   PDBsum; 7CKQ; -.
DR   PDBsum; 7F75; -.
DR   AlphaFoldDB; P20429; -.
DR   SMR; P20429; -.
DR   IntAct; P20429; 4.
DR   MINT; P20429; -.
DR   STRING; 224308.BSU01430; -.
DR   jPOST; P20429; -.
DR   PaxDb; P20429; -.
DR   PRIDE; P20429; -.
DR   EnsemblBacteria; CAB11919; CAB11919; BSU_01430.
DR   GeneID; 64301981; -.
DR   GeneID; 938921; -.
DR   KEGG; bsu:BSU01430; -.
DR   PATRIC; fig|224308.179.peg.147; -.
DR   eggNOG; COG0202; Bacteria.
DR   InParanoid; P20429; -.
DR   OMA; LMKFRNF; -.
DR   PhylomeDB; P20429; -.
DR   BioCyc; BSUB:BSU01430-MON; -.
DR   EvolutionaryTrace; P20429; -.
DR   PRO; PR:P20429; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.170.120.12; -; 1.
DR   Gene3D; 3.30.1360.10; -; 1.
DR   HAMAP; MF_00059; RNApol_bact_RpoA; 1.
DR   InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR   InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR   InterPro; IPR011773; DNA-dir_RpoA.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR011260; RNAP_asu_C.
DR   InterPro; IPR036643; RNApol_insert_sf.
DR   PANTHER; PTHR32108; PTHR32108; 1.
DR   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF03118; RNA_pol_A_CTD; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   SUPFAM; SSF56553; SSF56553; 1.
DR   TIGRFAMs; TIGR02027; rpoA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..314
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175265"
FT   REGION          1..228
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          245..314
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   STRAND          8..14
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:6WVK"
FT   STRAND          20..28
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   HELIX           32..44
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          49..58
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:6WVK"
FT   HELIX           75..82
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          95..108
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          118..121
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          135..149
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          173..185
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          188..200
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   HELIX           206..225
FT                   /evidence="ECO:0007829|PDB:6WVJ"
FT   HELIX           246..249
FT                   /evidence="ECO:0007829|PDB:1Z3E"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:1Z3E"
FT   HELIX           260..268
FT                   /evidence="ECO:0007829|PDB:1Z3E"
FT   HELIX           274..278
FT                   /evidence="ECO:0007829|PDB:1Z3E"
FT   HELIX           282..286
FT                   /evidence="ECO:0007829|PDB:1Z3E"
FT   HELIX           293..305
FT                   /evidence="ECO:0007829|PDB:1Z3E"
SQ   SEQUENCE   314 AA;  34799 MW;  9ADCAD891C0BCD67 CRC64;
     MIEIEKPKIE TVEISDDAKF GKFVVEPLER GYGTTLGNSL RRILLSSLPG AAVTSIQIDG
     VLHEFSTIEG VVEDVTTIIL HIKKLALKIY SDEEKTLEID VQGEGTVTAA DITHDSDVEI
     LNPDLHIATL GENASFRVRL TAQRGRGYTP ADANKRDDQP IGVIPIDSIY TPVSRVSYQV
     ENTRVGQVAN YDKLTLDVWT DGSTGPKEAI ALGSKILTEH LNIFVGLTDE AQHAEIMVEK
     EEDQKEKVLE MTIEELDLSV RSYNCLKRAG INTVQELANK TEEDMMKVRN LGRKSLEEVK
     AKLEELGLGL RKDD
 
 
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