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PHOT_BACSU
ID   PHOT_BACSU              Reviewed;         261 AA.
AC   O34627;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Blue-light photoreceptor;
DE   AltName: Full=Photoactive flavo-yellow protein;
DE   AltName: Full=Phototropin homolog;
GN   Name=pfyP; Synonyms=ytvA; OrderedLocusNames=BSU30340;
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=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
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   [3]
RP   FUNCTION, COMPLEX SUGGESTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=11157946; DOI=10.1128/jb.183.4.1329-1338.2001;
RA   Akbar S., Gaidenko T.A., Kang C.M., O'Reilly M., Devine K.M., Price C.W.;
RT   "New family of regulators in the environmental signaling pathway which
RT   activates the general stress transcription factor sigma(B) of Bacillus
RT   subtilis.";
RL   J. Bacteriol. 183:1329-1338(2001).
RN   [4]
RP   CHARACTERIZATION, AND 3D-STRUCTURE MODELING OF 25-126.
RX   PubMed=11964249; DOI=10.1016/s0006-3495(02)75604-x;
RA   Losi A., Polverini E., Quest B., Gaertner W.;
RT   "First evidence for phototropin-related blue-light receptors in
RT   prokaryotes.";
RL   Biophys. J. 82:2627-2634(2002).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 20-147, SUBUNIT, AND FMN-BINDING
RP   AT CYS-62.
RX   PubMed=17764689; DOI=10.1016/j.jmb.2007.07.039;
RA   Moglich A., Moffat K.;
RT   "Structural basis for light-dependent signaling in the dimeric LOV domain
RT   of the photosensor YtvA.";
RL   J. Mol. Biol. 373:112-126(2007).
CC   -!- FUNCTION: Exhibits the same spectroscopical features and blue-light
CC       induced photochemistry as plants phototropins, with the reversible
CC       formation of a blue-shifted photoproduct, assigned to an FMN-cysteine
CC       thiol adduct. Although it is a positive regulator in the activation of
CC       the environmental signaling branch of the general stress transcription
CC       factor sigma-B, its precise role is undetermined.
CC       {ECO:0000269|PubMed:11157946}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17764689}.
CC   -!- PTM: FMN binds covalently to cysteine after exposure to blue light and
CC       this bond is spontaneously broken in the dark.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene have a twofold decreased
CC       response to salt and ethanol stress, and a somewhat reduced response to
CC       energy stress, indicating that PhoT is a positive regulator of sigma-B
CC       activity. It acts independently of both RsbRA and RsbRB (YkoB).
CC       {ECO:0000269|PubMed:11157946}.
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DR   EMBL; AF008220; AAC00382.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15012.1; -; Genomic_DNA.
DR   PIR; A70002; A70002.
DR   RefSeq; NP_390912.1; NC_000964.3.
DR   RefSeq; WP_004399022.1; NZ_JNCM01000036.1.
DR   PDB; 2MWG; NMR; -; A/B=2-261.
DR   PDB; 2PR5; X-ray; 1.45 A; A/B=20-147.
DR   PDB; 2PR6; X-ray; 1.95 A; A/B=20-147.
DR   PDB; 4GCZ; X-ray; 2.30 A; A/B=1-126.
DR   PDBsum; 2MWG; -.
DR   PDBsum; 2PR5; -.
DR   PDBsum; 2PR6; -.
DR   PDBsum; 4GCZ; -.
DR   AlphaFoldDB; O34627; -.
DR   BMRB; O34627; -.
DR   SASBDB; O34627; -.
DR   SMR; O34627; -.
DR   STRING; 224308.BSU30340; -.
DR   PaxDb; O34627; -.
DR   DNASU; 937254; -.
DR   EnsemblBacteria; CAB15012; CAB15012; BSU_30340.
DR   GeneID; 937254; -.
DR   KEGG; bsu:BSU30340; -.
DR   PATRIC; fig|224308.179.peg.3291; -.
DR   eggNOG; COG1366; Bacteria.
DR   eggNOG; COG2202; Bacteria.
DR   InParanoid; O34627; -.
DR   OMA; FWNELNI; -.
DR   PhylomeDB; O34627; -.
DR   BioCyc; BSUB:BSU30340-MON; -.
DR   EvolutionaryTrace; O34627; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.750.24; -; 1.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF01740; STAS; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromophore; Flavoprotein; FMN; Photoreceptor protein;
KW   Receptor; Reference proteome; Sensory transduction; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..261
FT                   /note="Blue-light photoreceptor"
FT                   /id="PRO_0000172004"
FT   DOMAIN          12..87
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          88..138
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          147..258
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   MOD_RES         62
FT                   /note="S-4a-FMN cysteine"
FT   HELIX           5..7
FT                   /evidence="ECO:0007829|PDB:4GCZ"
FT   HELIX           9..20
FT                   /evidence="ECO:0007829|PDB:4GCZ"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   HELIX           44..50
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   HELIX           62..65
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   HELIX           72..84
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   STRAND          88..95
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   STRAND          101..113
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   STRAND          116..125
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   HELIX           127..145
FT                   /evidence="ECO:0007829|PDB:2PR5"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   HELIX           168..183
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   HELIX           184..186
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   HELIX           202..218
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   STRAND          221..226
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   HELIX           229..238
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   HELIX           241..244
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:2MWG"
FT   HELIX           251..257
FT                   /evidence="ECO:0007829|PDB:2MWG"
SQ   SEQUENCE   261 AA;  29195 MW;  4AD6EB00B6BD27DD CRC64;
     MASFQSFGIP GQLEVIKKAL DHVRVGVVIT DPALEDNPIV YVNQGFVQMT GYETEEILGK
     NCRFLQGKHT DPAEVDNIRT ALQNKEPVTV QIQNYKKDGT MFWNELNIDP MEIEDKTYFV
     GIQNDITKQK EYEKLLEDSL TEITALSTPI VPIRNGISAL PLVGNLTEER FNSIVCTLTN
     ILSTSKDDYL IIDLSGLAQV NEQTADQIFK LSHLLKLTGT ELIITGIKPE LAMKMNKLDA
     NFSSLKTYSN VKDAVKVLPI M
 
 
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