ID   CAEB_MYCTO              Reviewed;         520 AA.
AC   P9WHR4; L0TBV4; P65821; Q10508;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Carboxylesterase B {ECO:0000303|PubMed:17428787};
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=caeB {ECO:0000303|PubMed:17428787}; OrderedLocusNames=MT2281;
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).
RN   [2]
RP   SUBCELLULAR LOCATION, AND NOMENCLATURE.
RX   PubMed=17428787; DOI=10.1074/jbc.m700035200;
RA   Lun S., Bishai W.R.;
RT   "Characterization of a novel cell wall-anchored protein with
RT   carboxylesterase activity required for virulence in Mycobacterium
RT   tuberculosis.";
RL   J. Biol. Chem. 282:18348-18356(2007).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17428787}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46566.1; -; Genomic_DNA.
DR   PIR; C70776; C70776.
DR   RefSeq; WP_003411484.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHR4; -.
DR   SMR; P9WHR4; -.
DR   ESTHER; myctu-ym23; AlphaBeta_hydrolase.
DR   EnsemblBacteria; AAK46566; AAK46566; MT2281.
DR   KEGG; mtc:MT2281; -.
DR   PATRIC; fig|83331.31.peg.2455; -.
DR   HOGENOM; CLU_013364_3_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..520
FT                   /note="Carboxylesterase B"
FT                   /id="PRO_0000428137"
FT   DOMAIN          105..403
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHR3"
FT   ACT_SITE        461
FT                   /evidence="ECO:0000250|UniProtKB:P9WHR3"
FT   ACT_SITE        488
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHR3"
SQ   SEQUENCE   520 AA;  55078 MW;  7D05F1533A4C6B91 CRC64;
     MAAMWRRRPL SSALLSFGLL LGGLPLAAPP LAGATEEPGA GQTPGAPVVA PQQSWNSCRE
     FIADTSEIRT ARCATVSVPV DYDQPGGTQA KLAVIRVPAT GQRFGALLVN PGGPGASAVD
     MVAAMAPAIA DTDILRHFDL VGFDPRGVGH STPALRCRTD AEFDAYRRDP MADYSPAGVT
     HVEQVYRQLA QDCVDRMGFS FLANIGTASV ARDMDMVRQA LGDDQINYLG YSYGTELGTA
     YLERFGTHVR AMVLDGAIDP AVSPIEESIS QMAGFQTAFN DYAADCARSP ACPLGTDSAQ
     WVNRYHALVD PLVQKPGKTS DPRGLSYADA TTGTINALYS PQRWKYLTSG LLGLQRGSDA
     GDLLVLADDY DGRDADGHYS NDQDAFNAVR CVDAPTPADP AAWVAADQRI RQVAPFLSYG
     QFTGSAPRDL CALWPVPATS TPHPAAPAGA GKVVVVSTTH DPATPYQSGV DLARQLGAPL
     ITFDGTQHTA VFDGNQCVDS AVMHYFLDGT LPPTSLRCAP