ID   CULP2_MYCTO             Reviewed;         230 AA.
AC   P9WP40; L0TAS9; P63881; Q50664;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
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=MT2358;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46643.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46643.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003411863.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP40; -.
DR   SMR; P9WP40; -.
DR   ESTHER; myctu-cutas2; Cutinase.
DR   EnsemblBacteria; AAK46643; AAK46643; MT2358.
DR   KEGG; mtc:MT2358; -.
DR   PATRIC; fig|83331.31.peg.2538; -.
DR   HOGENOM; CLU_040058_3_0_11; -.
DR   Proteomes; UP000001020; 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_0000427018"
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