ID   FRSA_ESCF3              Reviewed;         414 AA.
AC   B7LNG1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Esterase FrsA {ECO:0000255|HAMAP-Rule:MF_01063};
DE            EC=3.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01063};
GN   Name=frsA {ECO:0000255|HAMAP-Rule:MF_01063}; OrderedLocusNames=EFER_2739;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of esters. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01063};
CC   -!- SIMILARITY: Belongs to the FrsA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01063}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU928158; CAQ90234.1; -; Genomic_DNA.
DR   RefSeq; WP_000189564.1; NC_011740.1.
DR   AlphaFoldDB; B7LNG1; -.
DR   SMR; B7LNG1; -.
DR   ESTHER; ecoli-yafa; Duf_1100-R.
DR   EnsemblBacteria; CAQ90234; CAQ90234; EFER_2739.
DR   KEGG; efe:EFER_2739; -.
DR   HOGENOM; CLU_036819_0_0_6; -.
DR   OMA; NIPWVDH; -.
DR   OrthoDB; 721431at2; -.
DR   BioCyc; EFER585054:EFER_RS13810-MON; -.
DR   Proteomes; UP000000745; Chromosome.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01063; FrsA; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR043423; FrsA.
DR   InterPro; IPR010520; FrsA-like.
DR   Pfam; PF06500; FrsA-like; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Serine esterase.
FT   CHAIN           1..414
FT                   /note="Esterase FrsA"
FT                   /id="PRO_1000136518"
SQ   SEQUENCE   414 AA;  46936 MW;  712DFCE64D5BF1BF CRC64;
     MTQANLSETL FKPRFKHPET STLVRRFNHG AQPPVQSALD GKTIPHWYRM INRLMWIWRG
     VDPREILEVQ SRIVMSAAER TDNDLYDTVI GYRGGNWIYE WATQAMVWQQ KACAEEDPQL
     SGRHWLHAAT LYNIAAYPHL KGDDLAEQAQ ALSNRAYEEA AQRLPGTMRQ MEFTVPGGAP
     ITGFLHMPKG DGPFPTVLMC GGLDAMQTDY YSLYERYFAP RGIAMLTIDM PSVGFSSKRK
     LTQDSSLLHQ HVLKALPNVP WVDHTRVAAF GFRFGANVAV RLAYLESPRL KAVACLGPVV
     HTLLSDFKCQ QQVPEMYLDV LASRLGMHDA SDEALRVELN RYSLKVQGLL GRRCPTPMLS
     GYWKNDPFSP EEDSRLITSS SADGKLLEIP FNPVYRNFDK GLQEITSWIE KRLC