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 03-AUG-2022, entry version 136.
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}.
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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 AlphaFoldDB; Q08788; -.
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; BSU_03520.
DR GeneID; 938300; -.
DR KEGG; bsu:BSU03520; -.
DR PATRIC; fig|224308.179.peg.369; -.
DR eggNOG; COG3208; Bacteria.
DR InParanoid; Q08788; -.
DR OMA; ALCRLIC; -.
DR PhylomeDB; Q08788; -.
DR BioCyc; BSUB:BSU03520-MON; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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;
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:0007829|PDB:2K2Q"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:2K2Q"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:2K2Q"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:2K2Q"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2K2Q"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:2K2Q"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:2K2Q"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2K2Q"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:2K2Q"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:2K2Q"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:2K2Q"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2K2Q"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:2K2Q"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:2K2Q"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:2K2Q"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:2K2Q"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:2K2Q"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:2K2Q"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:2K2Q"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:2K2Q"
FT TURN 236..238
FT /evidence="ECO:0007829|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
