ID   CULP2_MYCBO             Reviewed;         230 AA.
AC   P63882; A0A1R3Y1K6; Q50664; X2BKP1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Probable carboxylesterase Culp2 {ECO:0000250|UniProtKB:P9WP41};
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:P9WP43};
DE   AltName: Full=Cutinase-like protein 2 {ECO:0000250|UniProtKB:P9WP41};
DE            Short=Culp2 {ECO:0000250|UniProtKB:P9WP41};
DE   Flags: Precursor;
GN   Name=cut2; OrderedLocusNames=BQ2027_MB2323;
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P9WP41}. Cell
CC       surface {ECO:0000250|UniProtKB:P9WP41}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU00935.1; -; Genomic_DNA.
DR   RefSeq; NP_855972.1; NC_002945.3.
DR   RefSeq; WP_003411863.1; NC_002945.4.
DR   AlphaFoldDB; P63882; -.
DR   SMR; P63882; -.
DR   ESTHER; myctu-cutas2; Cutinase.
DR   EnsemblBacteria; SIU00935; SIU00935; BQ2027_MB2323.
DR   PATRIC; fig|233413.5.peg.2547; -.
DR   OMA; DDPICNP; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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; IPR006311; TAT_signal.
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; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..32
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           33..230
FT                   /note="Probable carboxylesterase Culp2"
FT                   /id="PRO_0000006448"
FT   ACT_SITE        123
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   ACT_SITE        207
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   DISULFID        45..112
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   DISULFID        185..192
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
SQ   SEQUENCE   230 AA;  23926 MW;  3707CA5016AEE5A3 CRC64;
     MNDLLTRRLL TMGAAAAMLA AVLLLTPITV PAGYPGAVAP ATAACPDAEV VFARGRFEPP
     GIGTVGNAFV SALRSKVNKN VGVYAVKYPA DNQIDVGAND MSAHIQSMAN SCPNTRLVPG
     GYSLGAAVTD VVLAVPTQMW GFTNPLPPGS DEHIAAVALF GNGSQWVGPI TNFSPAYNDR
     TIELCHGDDP VCHPADPNTW EANWPQHLAG AYVSSGMVNQ AADFVAGKLQ