ID   CULP3_MYCTU             Reviewed;         262 AA.
AC   P9WP39; 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 44.
DE   RecName: Full=Probable carboxylesterase Culp3 {ECO:0000305};
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:P9WP43};
DE   AltName: Full=Cutinase-like protein 3 {ECO:0000303|PubMed:19225166};
DE            Short=Culp3 {ECO:0000303|PubMed:19225166};
DE   Flags: Precursor;
GN   Name=cut3; OrderedLocusNames=Rv3451; ORFNames=MTCY13E12.04;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION.
RC   STRAIN=H37Rv;
RX   PubMed=19225166; DOI=10.1096/fj.08-114421;
RA   West N.P., Chow F.M., Randall E.J., Wu J., Chen J., Ribeiro J.M.,
RA   Britton W.J.;
RT   "Cutinase-like proteins of Mycobacterium tuberculosis: characterization of
RT   their variable enzymatic functions and active site identification.";
RL   FASEB J. 23:1694-1704(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Shows weak esterase activity with the p-nitrophenol-linked
CC       aliphatic ester pNP-butyrate. Does not exhibit cutinase activity.
CC       {ECO:0000269|PubMed:19225166}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP46273.1; -; Genomic_DNA.
DR   PIR; H70564; H70564.
DR   RefSeq; NP_217968.2; NC_000962.3.
DR   RefSeq; WP_003418336.1; NZ_NVQJ01000065.1.
DR   AlphaFoldDB; P9WP39; -.
DR   SMR; P9WP39; -.
DR   STRING; 83332.Rv3451; -.
DR   ESTHER; myctu-cut3; Cutinase.
DR   PaxDb; P9WP39; -.
DR   DNASU; 887611; -.
DR   GeneID; 887611; -.
DR   KEGG; mtu:Rv3451; -.
DR   TubercuList; Rv3451; -.
DR   eggNOG; ENOG5030I1N; Bacteria.
DR   OMA; PRHVPGK; -.
DR   PhylomeDB; P9WP39; -.
DR   Proteomes; UP000001584; 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   1: Evidence at protein level;
KW   Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW   Signal.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..262
FT                   /note="Probable carboxylesterase Culp3"
FT                   /id="PRO_0000006451"
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;  26504 MW;  1DE666FA938D3639 CRC64;
     MNNRPIRLLT SGRAGLGAGA LITAVVLLIA LGAVWTPVAF ADGCPDAEVT FARGTGEPPG
     IGRVGQAFVD SLRQQTGMEI GVYPVNYAAS RLQLHGGDGA NDAISHIKSM ASSCPNTKLV
     LGGYSQGATV IDIVAGVPLG SISFGSPLPA AYADNVAAVA VFGNPSNRAG GSLSSLSPLF
     GSKAIDLCNP TDPICHVGPG NEFSGHIDGY IPTYTTQAAS FVVQRLRAGS VPHLPGSVPQ
     LPGSVLQMPG TAAPAPESLH GR