AES_SHIFL
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-MAY-2022, entry version 110.
DE RecName: Full=Acetyl esterase {ECO:0000255|HAMAP-Rule:MF_01958};
DE EC=3.1.1.- {ECO:0000255|HAMAP-Rule:MF_01958};
GN Name=aes {ECO:0000255|HAMAP-Rule:MF_01958};
GN OrderedLocusNames=SF0421, S0428;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., 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 PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Displays esterase activity towards short chain fatty esters
CC (acyl chain length of up to 8 carbons). Able to hydrolyze
CC triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but
CC not trioleylglycerol (triolein) or cholesterol oleate. Negatively
CC regulates MalT activity by antagonizing maltotriose binding. Inhibits
CC MelA galactosidase activity. {ECO:0000255|HAMAP-Rule:MF_01958}.
CC -!- SUBUNIT: Homodimer. Interacts with MalT and MelA. {ECO:0000255|HAMAP-
CC Rule:MF_01958}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01958}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000255|HAMAP-Rule:MF_01958}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN42076.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP15953.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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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; WP_000801841.1; NZ_UIPM01000019.1.
DR AlphaFoldDB; Q83M39; -.
DR SMR; Q83M39; -.
DR STRING; 198214.SF0421; -.
DR ESTHER; shifl-AES; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A47; -.
DR EnsemblBacteria; AAN42076; AAN42076; SF0421.
DR EnsemblBacteria; AAP15953; AAP15953; S0428.
DR GeneID; 1027722; -.
DR KEGG; sfl:SF0421; -.
DR KEGG; sft:NCTC1_00435; -.
DR KEGG; sfx:S0428; -.
DR PATRIC; fig|198214.7.peg.483; -.
DR HOGENOM; CLU_012494_6_4_6; -.
DR OrthoDB; 1361074at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_01958; Acetyl_esterase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR023508; Acetyl_esterase.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..319
FT /note="Acetyl esterase"
FT /id="PRO_0000239713"
FT MOTIF 91..93
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01958"
FT ACT_SITE 262
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01958"
FT ACT_SITE 292
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01958"
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
