AES_SALTY
ID AES_SALTY Reviewed; 323 AA.
AC Q8ZRA1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
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}; OrderedLocusNames=STM0490;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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}.
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DR EMBL; AE006468; AAL19444.1; -; Genomic_DNA.
DR RefSeq; NP_459485.1; NC_003197.2.
DR RefSeq; WP_000801786.1; NC_003197.2.
DR PDB; 3GA7; X-ray; 1.55 A; A=1-323.
DR PDBsum; 3GA7; -.
DR AlphaFoldDB; Q8ZRA1; -.
DR SMR; Q8ZRA1; -.
DR STRING; 99287.STM0490; -.
DR ESTHER; salty-AES; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A47; -.
DR PaxDb; Q8ZRA1; -.
DR EnsemblBacteria; AAL19444; AAL19444; STM0490.
DR GeneID; 1252010; -.
DR KEGG; stm:STM0490; -.
DR PATRIC; fig|99287.12.peg.524; -.
DR HOGENOM; CLU_012494_6_4_6; -.
DR OMA; LWYPSTM; -.
DR PhylomeDB; Q8ZRA1; -.
DR BioCyc; SENT99287:STM0490-MON; -.
DR EvolutionaryTrace; Q8ZRA1; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
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; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..323
FT /note="Acetyl esterase"
FT /id="PRO_0000239711"
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"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 37..51
FT /evidence="ECO:0007829|PDB:3GA7"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3GA7"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3GA7"
FT STRAND 72..82
FT /evidence="ECO:0007829|PDB:3GA7"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3GA7"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:3GA7"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:3GA7"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3GA7"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:3GA7"
FT TURN 148..153
FT /evidence="ECO:0007829|PDB:3GA7"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 166..181
FT /evidence="ECO:0007829|PDB:3GA7"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:3GA7"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:3GA7"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:3GA7"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:3GA7"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:3GA7"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:3GA7"
FT HELIX 302..320
FT /evidence="ECO:0007829|PDB:3GA7"
SQ SEQUENCE 323 AA; 36799 MW; 91A9A4EF1CCA1A45 CRC64;
MKPENKIPVL TRLSDEMTAV VNFQQPGLPP WPADGDIETQ RQYYLLERRF WNADAPSMTT
RTCAVPTPYG DVTTRLYSPQ PTSQATLYYL HGGGFILGNL DTHDRIMRLL ARYTGCTVIG
IDYSLSPQAR YPQAIEETVA VCSYFSQHAD EYSLNVEKIG FAGDSAGAML ALASALWLRD
KHIRCGNVIA ILLWYGLYGL QDSVSRRLFG GAWDGLTRED LDMYEKAYLR NDEDRESPWY
CLFNNDLTRD VPPCFIASAE FDPLIDDSRL LHQTLQAHQQ PCEYKMYPGT LHAFLHYSRM
MTIADDALQD GARFFMARMK TPR
