FRSA_ECOHS
ID FRSA_ECOHS Reviewed; 414 AA.
AC A7ZWK2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=EcHS_A0266;
OS Escherichia coli O9:H4 (strain HS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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}.
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DR EMBL; CP000802; ABV04656.1; -; Genomic_DNA.
DR RefSeq; WP_000189543.1; NC_009800.1.
DR AlphaFoldDB; A7ZWK2; -.
DR SMR; A7ZWK2; -.
DR ESTHER; ecoli-yafa; Duf_1100-R.
DR GeneID; 66671443; -.
DR KEGG; ecx:EcHS_A0266; -.
DR HOGENOM; CLU_036819_0_0_6; -.
DR OMA; NIPWVDH; -.
DR Proteomes; UP000001123; 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_1000064478"
SQ SEQUENCE 414 AA; 46965 MW; 48783F168ADD57CB CRC64;
MTQANLSETL FKPRFKHPET STLVRRFNHG 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 KAVACLGPVV
HTLLSDFKCQ QQVPEMYLDV LASRLGMHDA SDEALRVELN RYSLKVQGLL GRRCPTPMLS
GYWKNDPFSP EEDSRLITSS SADGKLLEIP FNPVYRNFDK GLQEITGWIE KRLC