(data stored in ACNUC7421 zone)

SWISSPROT: SRFAD_BACSU

ID   SRFAD_BACSU             Reviewed;         242 AA.
AC   Q08788;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 126.
DE   RecName: Full=Surfactin synthase thioesterase subunit;
DE            EC=3.1.2.-;
DE   AltName: Full=Cold shock protein CSI16;
GN   Name=srfAD; Synonyms=srfA4; OrderedLocusNames=BSU03520;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8355609; DOI=10.1111/j.1365-2958.1993.tb01629.x;
RA   Cosmina P., Rodriguez F., de Ferra F., Grandi G., Perego M., Venema G.,
RA   van Sinderen D.;
RT   "Sequence and analysis of the genetic locus responsible for surfactin
RT   synthesis in Bacillus subtilis.";
RL   Mol. Microbiol. 8:821-831(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(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   PROTEIN SEQUENCE OF 2-27.
RC   STRAIN=168 / JH642;
RA   Graumann P.L., Schmid R., Marahiel M.A.;
RL   Submitted (OCT-1997) to UniProtKB.
CC   -!- FUNCTION: Probable thioesterase involved in the biosynthesis of
CC       surfactin.
CC   -!- PATHWAY: Antibiotic biosynthesis; surfactin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: In response to low temperature.
CC   -!- SIMILARITY: Belongs to the thioesterase family. {ECO:0000305}.
DR   EMBL; X70356; CAA49819.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08986.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12146.1; -; Genomic_DNA.
DR   PIR; I40488; I40488.
DR   RefSeq; NP_388234.1; NC_000964.3.
DR   RefSeq; WP_003234568.1; NZ_JNCM01000031.1.
DR   PDB; 2K2Q; NMR; -; B=1-242.
DR   PDB; 2RON; NMR; -; A=1-242.
DR   PDBsum; 2K2Q; -.
DR   PDBsum; 2RON; -.
DR   SMR; Q08788; -.
DR   DIP; DIP-59839N; -.
DR   IntAct; Q08788; 1.
DR   STRING; 224308.BSU03520; -.
DR   ESTHER; bacsu-srf4; Thioesterase.
DR   MEROPS; S33.A03; -.
DR   jPOST; Q08788; -.
DR   PaxDb; Q08788; -.
DR   PRIDE; Q08788; -.
DR   DNASU; 938300; -.
DR   EnsemblBacteria; CAB12146; CAB12146; BSU03520.
DR   GeneID; 938300; -.
DR   KEGG; bsu:BSU03520; -.
DR   PATRIC; fig|224308.179.peg.369; -.
DR   eggNOG; COG3208; LUCA.
DR   HOGENOM; HOG000131891; -.
DR   InParanoid; Q08788; -.
DR   KO; K15657; -.
DR   OMA; FRLICFP; -.
DR   PhylomeDB; Q08788; -.
DR   BioCyc; BSUB:BSU03520-MONOMER; -.
DR   SABIO-RK; Q08788; -.
DR   UniPathway; UPA00181; -.
DR   EvolutionaryTrace; Q08788; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012223; TEII.
DR   InterPro; IPR001031; Thioesterase.
DR   PANTHER; PTHR11487; PTHR11487; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q08788.
DR   SWISS-2DPAGE; Q08788.
KW   3D-structure; Antibiotic biosynthesis; Cytoplasm;
KW   Direct protein sequencing; Hydrolase; Reference proteome; Sporulation;
KW   Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CHAIN           2..242
FT                   /note="Surfactin synthase thioesterase subunit"
FT                   /id="PRO_0000180364"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000250"
FT   CONFLICT        12
FT                   /note="E -> N (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..5
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   STRAND          15..19
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   HELIX           24..36
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   STRAND          43..46
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   TURN            57..59
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   HELIX           60..67
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   TURN            68..71
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   STRAND          81..83
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   HELIX           90..103
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   STRAND          108..115
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   HELIX           130..134
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   TURN            145..147
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   HELIX           148..151
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   TURN            152..155
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   HELIX           160..167
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   STRAND          181..187
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   HELIX           193..201
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   STRAND          207..213
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   HELIX           218..222
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   HELIX           224..235
FT                   /evidence="ECO:0000244|PDB:2K2Q"
FT   TURN            236..238
FT                   /evidence="ECO:0000244|PDB:2K2Q"
SQ   SEQUENCE   242 AA;  27621 MW;  532C702F972B2059 CRC64;
     MSQLFKSFDA SEKTQLICFP FAGGYSASFR PLHAFLQGEC EMLAAEPPGH GTNQTSAIED
     LEELTDLYKQ ELNLRPDRPF VLFGHSMGGM ITFRLAQKLE REGIFPQAVI ISAIQPPHIQ
     RKKVSHLPDD QFLDHIIQLG GMPAELVENK EVMSFFLPSF RSDYRALEQF ELYDLAQIQS
     PVHVFNGLDD KKCIRDAEGW KKWAKDITFH QFDGGHMFLL SQTEEVAERI FAILNQHPII
     QP
//

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