ID   CULP1_MYCBO             Reviewed;         217 AA.
AC   P63880; A0A1R3XZY4; Q10837; X2BJ73;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Carboxylesterase Culp1 {ECO:0000250|UniProtKB:P9WP43};
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:P9WP43};
DE   AltName: Full=Cutinase-like protein 1 {ECO:0000250|UniProtKB:P9WP43};
DE            Short=Culp1 {ECO:0000250|UniProtKB:P9WP43};
DE   Flags: Precursor;
GN   OrderedLocusNames=BQ2027_MB2006C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Shows esterase activity, with a preference for short- and
CC       medium-chain fatty acids. {ECO:0000250|UniProtKB:P9WP43}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol
CC         + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748;
CC         Evidence={ECO:0000250|UniProtKB:P9WP43};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59389;
CC         Evidence={ECO:0000250|UniProtKB:P9WP43};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P9WP43}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU00612.1; -; Genomic_DNA.
DR   RefSeq; NP_855656.1; NC_002945.3.
DR   RefSeq; WP_003409976.1; NC_002945.4.
DR   AlphaFoldDB; P63880; -.
DR   SMR; P63880; -.
DR   ESTHER; myctu-cutas1; Cutinase.
DR   EnsemblBacteria; SIU00612; SIU00612; BQ2027_MB2006C.
DR   GeneID; 45425962; -.
DR   PATRIC; fig|233413.5.peg.2203; -.
DR   OMA; TYPMDGS; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000675; Cutinase/axe.
DR   InterPro; IPR043580; CUTINASE_1.
DR   InterPro; IPR043579; CUTINASE_2.
DR   PANTHER; PTHR33630; PTHR33630; 1.
DR   Pfam; PF01083; Cutinase; 1.
DR   SMART; SM01110; Cutinase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00155; CUTINASE_1; 1.
DR   PROSITE; PS00931; CUTINASE_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..217
FT                   /note="Carboxylesterase Culp1"
FT                   /id="PRO_0000006446"
FT   ACT_SITE        118
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP43"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000250|UniProtKB:P9WP43"
FT   ACT_SITE        193
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP43"
FT   SITE            119
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        35..107
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   DISULFID        177..184
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
SQ   SEQUENCE   217 AA;  21782 MW;  500589547B9A87B0 CRC64;
     MTPRSLVRIV GVVVATTLAL VSAPAGGRAA HADPCSDIAV VFARGTHQAS GLGDVGEAFV
     DSLTSQVGGR SIGVYAVNYP ASDDYRASAS NGSDDASAHI QRTVASCPNT RIVLGGYSQG
     ATVIDLSTSA MPPAVADHVA AVALFGEPSS GFSSMLWGGG SLPTIGPLYS SKTINLCAPD
     DPICTGGGNI MAHVSYVQSG MTSQAATFAA NRLDHAG