ID   AES_SHIFL               Reviewed;         319 AA.
AC   Q83M39; Q7C2W8;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   25-JAN-2012, entry version 57.
DE   RecName: Full=Acetyl esterase;
DE            EC=3.1.1.-;
GN   Name=aes; OrderedLocusNames=SF0421, S0428;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   MEDLINE=22590274; PubMed=12704152;
RX   DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Displays esterase activity towards short chain fatty
CC       esters (acyl chain length of up to 8 carbons). Able to hydrolyze
CC       triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin),
CC       but not trioleylglycerol (triolein) or cholesterol oleate.
CC       Negatively regulates malT activity by antagonizing maltotriose
CC       binding. Inhibits melA galactosidase activity (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with malT and melA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN42076.1; Type=Erroneous termination; Positions=273; Note=Translated as Gln;
CC       Sequence=AAP15953.1; Type=Erroneous termination; Positions=273; Note=Translated as Gln;
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DR   EMBL; AE005674; AAN42076.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE014073; AAP15953.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_706369.1; NC_004337.2.
DR   RefSeq; NP_836147.1; NC_004741.1.
DR   ProteinModelPortal; Q83M39; -.
DR   EnsemblBacteria; EBESCT00000086030; EBESCP00000082852; EBESCG00000085075.
DR   EnsemblBacteria; EBESCT00000092883; EBESCP00000089519; EBESCG00000091927.
DR   GeneID; 1027722; -.
DR   GeneID; 1076865; -.
DR   GenomeReviews; AE005674_GR; SF0421.
DR   GenomeReviews; AE014073_GR; S0428.
DR   KEGG; sfl:SF0421; -.
DR   KEGG; sfx:S0428; -.
DR   PATRIC; 18701879; VBIShiFle31049_0472.
DR   GeneTree; EBGT00050000009160; -.
DR   HOGENOM; HBG757640; -.
DR   BioCyc; SFLE198214:AAN42076.1-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   HAMAP; MF_01958; Acetyl_esterase; 1; -.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR023508; Acetyl_esterase_GDXG_lipolytic.
DR   InterPro; IPR002168; Lipase_GDXG_AS.
DR   KO; K01066; -.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Serine esterase.
FT   CHAIN         1    319       Acetyl esterase.
FT                                /FTId=PRO_0000239713.
FT   ACT_SITE    165    165       By similarity.
FT   ACT_SITE    262    262       By similarity.
FT   ACT_SITE    292    292       By similarity.
SQ   SEQUENCE   319 AA;  36037 MW;  A61E91C47CEB35D6 CRC64;
     MKPENKLPVL DLISAEMKTV VNTLQPDLPS WPATGTIAEQ RQYYTLERRF WNAGAPEMAT
     RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
     INYTLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD
     KQIDCGKIAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
     CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
     MKTADEALRD GAQFFTAQL
//