ID   ESTR_MYCTO              Reviewed;         456 AA.
AC   P9WM38; L0T8Y0; Q10614;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Esterase MT1326 {ECO:0000250|UniProtKB:P9WM39};
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:P9WM39};
GN   OrderedLocusNames=MT1326;
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).
CC   -!- FUNCTION: Exhibits lipolytic activity with medium chain length esters
CC       as optimum substrates. {ECO:0000250|UniProtKB:P9WM39}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol
CC         + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748;
CC         Evidence={ECO:0000250|UniProtKB:P9WM39};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000250|UniProtKB:P9WM39}. Note=Cell wall anchored. Binds
CC       peptidoglycans via the LytM domains. {ECO:0000250|UniProtKB:P9WM39}.
CC   -!- DOMAIN: Contains an N-terminal LytE region, which consists of three
CC       consecutive LysM domains, and a C-terminal esterase domain. LytM
CC       domains are essential for anchoring protein to the cell wall.
CC       {ECO:0000250|UniProtKB:P9WM39}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45587.1; -; Genomic_DNA.
DR   PIR; D70772; D70772.
DR   RefSeq; WP_003406625.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WM38; -.
DR   SMR; P9WM38; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   ESTHER; myctu-yc88; A85-Mycolyl-transferase.
DR   EnsemblBacteria; AAK45587; AAK45587; MT1326.
DR   KEGG; mtc:MT1326; -.
DR   PATRIC; fig|83331.31.peg.1432; -.
DR   HOGENOM; CLU_026624_2_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 3.
DR   Gene3D; 3.10.350.10; -; 3.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000801; Esterase-like.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   Pfam; PF00756; Esterase; 1.
DR   Pfam; PF01476; LysM; 3.
DR   SMART; SM00257; LysM; 3.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   PROSITE; PS51782; LYSM; 3.
PE   3: Inferred from homology;
KW   Cell wall; Hydrolase; Lipid metabolism; Repeat; Secreted; Serine esterase.
FT   CHAIN           1..456
FT                   /note="Esterase MT1326"
FT                   /id="PRO_0000427371"
FT   DOMAIN          3..50
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          54..101
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          105..152
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000250|UniProtKB:P9WM39"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000250|UniProtKB:P9WM39"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000250|UniProtKB:P9WM39"
SQ   SEQUENCE   456 AA;  49619 MW;  9B70C0471EDF113A CRC64;
     MVSTHAVVAG ETLSALALRF YGDAELYRLI AAASGIADPD VVNVGQRLIM PDFTRYTVVA
     GDTLSALALR FYGDAELNWL IAAASGIADP DVVNVGQRLI MPDFTRYTVV AGDTLSALAA
     RFYGDASLYP LIAAVNGIAD PGVIDVGQVL VIFIGRSDGF GLRIVDRNEN DPRLWYYRFQ
     TSAIGWNPGV NVLLPDDYRT SGRTYPVLYL FHGGGTDQDF RTFDFLGIRD LTAGKPIIIV
     MPDGGHAGWY SNPVSSFVGP RNWETFHIAQ LLPWIEANFR TYAEYDGRAV AGFSMGGFGA
     LKYAAKYYGH FASASSHSGP ASLRRDFGLV VHWANLSSAV LDLGGGTVYG APLWDQARVS
     ADNPVERIDS YRNKRIFLVA GTSPDPANWF DSVNETQVLA GQREFRERLS NAGIPHESHE
     VPGGHVFRPD MFRLDLDGIV ARLRPASIGA AAERAD