位置:首页 > 蛋白库 > PKSS_BACSU
PKSS_BACSU
ID   PKSS_BACSU              Reviewed;         405 AA.
AC   O31785;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Polyketide biosynthesis cytochrome P450 PksS;
DE            EC=1.14.-.-;
GN   Name=pksS; OrderedLocusNames=BSU17230;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [3]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=168;
RX   PubMed=17482575; DOI=10.1016/j.bbrc.2007.04.151;
RA   Reddick J.J., Antolak S.A., Raner G.M.;
RT   "PksS from Bacillus subtilis is a cytochrome P450 involved in bacillaene
RT   metabolism.";
RL   Biochem. Biophys. Res. Commun. 358:363-367(2007).
CC   -!- FUNCTION: Involved in the metabolism of the antibiotic polyketide
CC       bacillaene which is involved in secondary metabolism. The substrate is
CC       dihydrobacillaene. {ECO:0000269|PubMed:17482575}.
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL009126; CAB13607.2; -; Genomic_DNA.
DR   RefSeq; NP_389605.2; NC_000964.3.
DR   RefSeq; WP_003244857.1; NZ_JNCM01000035.1.
DR   PDB; 4YZR; X-ray; 1.35 A; A=1-405.
DR   PDBsum; 4YZR; -.
DR   AlphaFoldDB; O31785; -.
DR   SMR; O31785; -.
DR   STRING; 224308.BSU17230; -.
DR   PaxDb; O31785; -.
DR   PRIDE; O31785; -.
DR   EnsemblBacteria; CAB13607; CAB13607; BSU_17230.
DR   GeneID; 940046; -.
DR   KEGG; bsu:BSU17230; -.
DR   PATRIC; fig|224308.179.peg.1868; -.
DR   eggNOG; COG2124; Bacteria.
DR   InParanoid; O31785; -.
DR   OMA; NCIFLLN; -.
DR   PhylomeDB; O31785; -.
DR   BioCyc; BSUB:BSU17230-MON; -.
DR   UniPathway; UPA01003; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic biosynthesis; Cell membrane; Heme; Iron; Membrane;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..405
FT                   /note="Polyketide biosynthesis cytochrome P450 PksS"
FT                   /id="PRO_0000380708"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         352
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   HELIX           11..15
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           17..27
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          29..35
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          42..47
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           50..58
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           85..88
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           98..106
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           112..116
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           119..133
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          136..140
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           141..144
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   TURN            145..147
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           148..158
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           165..175
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           183..206
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           212..218
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           228..259
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           261..269
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           271..273
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           274..285
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          295..298
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          305..307
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          312..315
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           317..320
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   TURN            324..326
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           355..372
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   HELIX           382..384
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          391..393
FT                   /evidence="ECO:0007829|PDB:4YZR"
FT   STRAND          400..402
FT                   /evidence="ECO:0007829|PDB:4YZR"
SQ   SEQUENCE   405 AA;  46729 MW;  99AD907CC96DD161 CRC64;
     MEKLMFHPHG KEFHHNPFSV LGRFREEEPI HRFELKRFGA TYPAWLITRY DDCMAFLKDN
     RITRDVKNVM NQEQIKMLNV SEDIDFVSDH MLAKDTPDHT RLRSLVHQAF TPRTIENLRG
     SIEQIAEQLL DEMEKENKAD IMKSFASPLP FIVISELMGI PKEDRSQFQI WTNAMVDTSE
     GNRELTNQAL REFKDYIAKL IHDRRIKPKD DLISKLVHAE ENGSKLSEKE LYSMLFLLVV
     AGLETTVNLL GSGTLALLQH KKECEKLKQQ PEMIATAVEE LLRYTSPVVM MANRWAIEDF
     TYKGHSIKRG DMIFIGIGSA NRDPNFFENP EILNINRSPN RHISFGFGIH FCLGAPLARL
     EGHIAFKALL KRFPDIELAV APDDIQWRKN VFLRGLESLP VSLSK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024