ID   FRSA_PECAS              Reviewed;         416 AA.
AC   Q6D1I1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=ECA3465;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG76364.1; -; Genomic_DNA.
DR   RefSeq; WP_011094973.1; NC_004547.2.
DR   AlphaFoldDB; Q6D1I1; -.
DR   SMR; Q6D1I1; -.
DR   STRING; 218491.ECA3465; -.
DR   ESTHER; erwct-Y3465; Duf_1100-R.
DR   EnsemblBacteria; CAG76364; CAG76364; ECA3465.
DR   GeneID; 57210134; -.
DR   KEGG; eca:ECA3465; -.
DR   PATRIC; fig|218491.5.peg.3505; -.
DR   eggNOG; COG1073; Bacteria.
DR   HOGENOM; CLU_036819_0_0_6; -.
DR   OMA; NIPWVDH; -.
DR   OrthoDB; 721431at2; -.
DR   Proteomes; UP000007966; 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; Reference proteome; Serine esterase.
FT   CHAIN           1..416
FT                   /note="Esterase FrsA"
FT                   /id="PRO_1000064483"
FT   REGION          19..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  47062 MW;  FBE9E0176DE1005F CRC64;
     MAQANLSETL FKPSFKHRET STLVRRTRHD QETQGLHSTL EGEKTSSWYR MINRLMWIWR
     GVNPWEIEDV LSRIAASQAD RSNEQLLDTV IGYRGGNWIY EWAKQGADWQ QRATESGDDA
     QTGQFWLNAA NLYSIAAYPH IKGDELAEQA QTLANRAYEE AAKYLPYELK ELTFPIAGGG
     TLTGFLHMPS QGKAPFPTVL MCGSLETLQS DYHRLFQDYF APAGMAMLTI DVPSVGFSSR
     WKLTQDSSFL HQQVLRALPD VPWVDHCRVT AFGFRFGANI AVRLAYLESQ RLRGVACLGP
     VVHHLLSDPN RQQQVPDMFM DVLASRLGMP FSTDASLKTE LGRYSLKTQG LLGRRCPTPM
     LAGYWENDLL CPKEEASLIV NSSAQGKLMP VNFSPVYQNF DRALQQISRW LQDKVC