ID   CULP7_MYCTU             Reviewed;         187 AA.
AC   Q79FA4; I6X868; L0TGB9;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Probable carboxylesterase Culp7 {ECO:0000305};
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:P9WP43};
DE   AltName: Full=Cutinase-like protein 7 {ECO:0000303|PubMed:19225166};
DE            Short=Culp7 {ECO:0000303|PubMed:19225166};
GN   Name=cut5b {ECO:0000312|EMBL:CCP46551.1};
GN   OrderedLocusNames=Rv3724B {ECO:0000312|EMBL:CCP46551.1};
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   SHOWS THAT IT DOES NOT HAVE CUTINASE ACTIVITY.
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   EXPRESSION, FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=H37Rv;
RX   PubMed=26177502; DOI=10.1371/journal.pone.0133186;
RA   Verma D., Das L., Gambhir V., Dikshit K.L., Varshney G.C.;
RT   "Heterogeneity among homologs of cutinase-like protein Cut5 in
RT   Mycobacteria.";
RL   PLoS ONE 10:e0133186-e0133186(2015).
CC   -!- FUNCTION: May have a role in cell wall processes (PubMed:26177502).
CC       Does not exhibit cutinase activity (PubMed:19225166).
CC       {ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:26177502}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26177502}. Cell
CC       membrane {ECO:0000269|PubMed:26177502}. Secreted, cell wall
CC       {ECO:0000269|PubMed:26177502}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at late exponential and stationary
CC       phases, but not in the early exponential phase.
CC       {ECO:0000269|PubMed:26177502}.
CC   -!- MISCELLANEOUS: A single nucleotide (T) insertion is observed in the
CC       Rv3724/cut5 gene. Cut5 is expressed as Rv3724a/cut5a and Rv3724b/cut5b
CC       in H37Rv strain. {ECO:0000269|PubMed:26177502}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP46551.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q79FA4; -.
DR   SMR; Q79FA4; -.
DR   STRING; 83332.Rv3724B; -.
DR   ESTHER; myctu-RV3724; Cutinase.
DR   PaxDb; Q79FA4; -.
DR   PRIDE; Q79FA4; -.
DR   PATRIC; fig|83332.111.peg.4141; -.
DR   TubercuList; Rv3724B; -.
DR   eggNOG; ENOG5030PZC; Bacteria.
DR   OMA; CPNTREV; -.
DR   PhylomeDB; Q79FA4; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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   PANTHER; PTHR33630; PTHR33630; 1.
DR   Pfam; PF01083; Cutinase; 1.
DR   SMART; SM01110; Cutinase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell wall; Cytoplasm; Disulfide bond; Hydrolase; Membrane;
KW   Reference proteome; Secreted; Serine esterase.
FT   CHAIN           1..187
FT                   /note="Probable carboxylesterase Culp7"
FT                   /id="PRO_0000450112"
FT   ACT_SITE        80
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   ACT_SITE        155
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   ACT_SITE        167
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   SITE            81
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        15..69
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   DISULFID        151..158
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
SQ   SEQUENCE   187 AA;  18787 MW;  741BCD8C568577DC CRC64;
     MAPGSHLVLA ASEDCSSTHC VSQVGAKSLG VYAVNYPASN DFASSDFPKT VIDGIRDAGS
     HIQSMAMSCP QTRQVLGGYS QGAAVAGYVT SAVVPPAVPV QAVPAPMAPE VANHVAAVTL
     FGAPSAQFLG QYGAPPIAIG PLYQPKTLQL CADGDSICGD GNSPVAHGLY AVNGMVGQGA
     NFAASRL