ID   CULP3_MYCTO             Reviewed;         262 AA.
AC   P9WP38; L0TCK2; O06318; P0A536;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Probable carboxylesterase Culp3 {ECO:0000250|UniProtKB:P9WP39};
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:P9WP43};
DE   AltName: Full=Cutinase-like protein 3 {ECO:0000250|UniProtKB:P9WP39};
DE            Short=Culp3 {ECO:0000250|UniProtKB:P9WP39};
DE   Flags: Precursor;
GN   Name=cut3; OrderedLocusNames=MT3557;
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:0000305}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47897.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK47897.1; ALT_INIT; Genomic_DNA.
DR   PIR; H70564; H70564.
DR   RefSeq; WP_015628936.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP38; -.
DR   SMR; P9WP38; -.
DR   ESTHER; myctu-cut3; Cutinase.
DR   EnsemblBacteria; AAK47897; AAK47897; MT3557.
DR   KEGG; mtc:MT3557; -.
DR   PATRIC; fig|83331.31.peg.3816; -.
DR   HOGENOM; CLU_040058_3_1_11; -.
DR   Proteomes; UP000001020; 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   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.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..262
FT                   /note="Probable carboxylesterase Culp3"
FT                   /id="PRO_0000427019"
FT   REGION          241..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        125
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   ACT_SITE        206
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   SITE            126
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        44..114
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   DISULFID        188..195
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
SQ   SEQUENCE   262 AA;  26578 MW;  60D98461EF6673C4 CRC64;
     MNNRPIRLLT SGRAGLGAGA LITAVVLLIA LGAVWTLVAF ADGCPDAEVT FARGTGEPPG
     IGRVGQAFVD SLRQQTGMEI GVYPVNYAAS RLQLHGGDGA NDAISHIKSM ASSCPNTKLV
     LGGYSQGATV IDIVAGVPLG SISFGSPLPA AYADNVAAVA VFGNPSNRAG GSLSSLSPLF
     GSKAIDLCNP TDPICHVGPG NEFSGHIDDY IPTYTTQAAS FVVQRLRAGS VPHLPGSVPQ
     LPGSVLQMPG TAAPAPESLH GR