CULP3_MYCBO
ID CULP3_MYCBO Reviewed; 262 AA.
AC P0A537; A0A1R3Y4A9; O06318; X2BNC9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=BQ2027_MB3481;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; LT708304; SIU02109.1; -; Genomic_DNA.
DR RefSeq; NP_857121.1; NC_002945.3.
DR RefSeq; WP_003418336.1; NC_002945.4.
DR AlphaFoldDB; P0A537; -.
DR SMR; P0A537; -.
DR ESTHER; myctu-cut3; Cutinase.
DR EnsemblBacteria; SIU02109; SIU02109; BQ2027_MB3481.
DR PATRIC; fig|233413.5.peg.3818; -.
DR OMA; PRHVPGK; -.
DR Proteomes; UP000001419; 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_0000006450"
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
