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Database: UniProt
Entry: S1PT37_ECOLX
LinkDB: S1PT37_ECOLX
Original site: S1PT37_ECOLX 
ID   S1PT37_ECOLX            Unreviewed;       414 AA.
AC   S1PT37;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Esterase FrsA {ECO:0000256|HAMAP-Rule:MF_01063};
DE            EC=3.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01063};
GN   Name=frsA {ECO:0000256|HAMAP-Rule:MF_01063};
GN   ORFNames=A13A_00270 {ECO:0000313|EMBL:EOX01434.1};
OS   Escherichia coli KTE182.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=1181728 {ECO:0000313|EMBL:EOX01434.1, ECO:0000313|Proteomes:UP000014179};
RN   [1] {ECO:0000313|EMBL:EOX01434.1, ECO:0000313|Proteomes:UP000014179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTE182 {ECO:0000313|EMBL:EOX01434.1,
RC   ECO:0000313|Proteomes:UP000014179};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Nielsen K.L., Frimodt-Moller N., Andersen P.S., Walker B.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Escherichia coli KTE182.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of esters. {ECO:0000256|HAMAP-
CC       Rule:MF_01063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01063};
CC   -!- SIMILARITY: Belongs to the FrsA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01063}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOX01434.1}.
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DR   EMBL; ASUG01000017; EOX01434.1; -; Genomic_DNA.
DR   RefSeq; WP_000189578.1; NZ_KE136858.1.
DR   AlphaFoldDB; S1PT37; -.
DR   SMR; S1PT37; -.
DR   PATRIC; fig|1181728.3.peg.263; -.
DR   HOGENOM; CLU_036819_0_0_6; -.
DR   Proteomes; UP000014179; Unassembled WGS sequence.
DR   GO; GO:0106435; F:carboxylesterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   HAMAP; MF_01063; FrsA; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR043423; FrsA.
DR   InterPro; IPR010520; FrsA-like.
DR   PANTHER; PTHR22946:SF4; DLH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22946; UNCHARACTERIZED; 1.
DR   Pfam; PF06500; FrsA-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01063};
KW   Serine esterase {ECO:0000256|ARBA:ARBA00022487, ECO:0000256|HAMAP-
KW   Rule:MF_01063}.
SQ   SEQUENCE   414 AA;  47024 MW;  DC63C8D46B0453E3 CRC64;
     MTQANLSETL FKPRFKHPET STLVRRFSHG AQPPVQSALD GKTIPHWYRM INRLMWIWRG
     IDPREILDVQ ARIVMSDAER TDDDLYDTVI GYRGGNWIYE WATQAMVWQQ KACAEEDPQL
     SGRHWLHAAT LYNIAAYPHL KGDDLAEQAQ ALSNRAYEEA AQRLPGTMRQ MEFTVPGGAP
     ITGFLHMPKG DGPFPTVLMC GGLDAMQTDY YSLYERYFAP RGIAMLTIDM PSVGFSSKWK
     LTQDSSLLHQ HVLKALPNVP WVDHTRVAAF GFRFGANVAV RLAYLESPRL KVVACLGPVV
     HTLLSDFKCQ QQVPEMYLDV LASRLGMHDA SDEALRVELN RYSLKVQGLL GRRCPTPMLS
     GYWKNDPFSP EEDSRLITSS SADGKLLEIP FNPVYRNFDK GLQEITDWIE KRLC
//
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