CULP5_MYCTU
ID CULP5_MYCTU Reviewed; 174 AA.
AC O06793; I6YBJ4; Q7D805;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Probable carboxylesterase Culp5 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000250|UniProtKB:P9WP43};
DE AltName: Full=Cutinase-like protein 5 {ECO:0000303|PubMed:19225166};
DE Short=Culp5 {ECO:0000303|PubMed:19225166};
GN Name=cut1 {ECO:0000312|EMBL:CCP44524.1};
GN OrderedLocusNames=Rv1758 {ECO:0000312|EMBL:CCP44524.1};
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).
CC -!- FUNCTION: Does not exhibit cutinase activity.
CC {ECO:0000269|PubMed:19225166}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44524.1; -; Genomic_DNA.
DR RefSeq; NP_216274.1; NC_000962.3.
DR RefSeq; WP_009934708.1; NC_000962.3.
DR AlphaFoldDB; O06793; -.
DR SMR; O06793; -.
DR STRING; 83332.Rv1758; -.
DR ESTHER; myctu-RV1758; Cutinase.
DR PaxDb; O06793; -.
DR DNASU; 885552; -.
DR GeneID; 885552; -.
DR KEGG; mtu:Rv1758; -.
DR PATRIC; fig|83332.111.peg.1956; -.
DR TubercuList; Rv1758; -.
DR eggNOG; ENOG5030PZC; Bacteria.
DR OMA; PPINIGH; -.
DR PhylomeDB; O06793; -.
DR Proteomes; UP000001584; Chromosome.
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 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..174
FT /note="Probable carboxylesterase Culp5"
FT /id="PRO_0000450108"
FT ACT_SITE 67
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT ACT_SITE 141
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT ACT_SITE 153
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT SITE 68
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 137..144
FT /evidence="ECO:0000250|UniProtKB:O53581"
SQ SEQUENCE 174 AA; 17868 MW; 36684DEB29AE73C8 CRC64;
MPGRFREDFI DALRSKIGEK SMGVYGVDYP ATTDFPTAMA GIYDAGTHVE QTAANCPQSK
LVLGGFSQGA AVMGFVTAAA IPDGAPLDAP RPMPPEVADH VAAVTLFGMP SVAFMHSIGA
PPIVIGPLYA EKTIQLCAPG DPVCSSGGNW AAHNGYADDG MVEQAAVFAA GRLG