ID   FRSA_SALPA              Reviewed;         414 AA.
AC   Q5PF65;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=SPA2437;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(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}.
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; CP000026; AAV78317.1; -; Genomic_DNA.
DR   RefSeq; WP_000189586.1; NC_006511.1.
DR   AlphaFoldDB; Q5PF65; -.
DR   SMR; Q5PF65; -.
DR   ESTHER; salty-yafa; Duf_1100-R.
DR   EnsemblBacteria; AAV78317; AAV78317; SPA2437.
DR   KEGG; spt:SPA2437; -.
DR   HOGENOM; CLU_036819_0_0_6; -.
DR   OMA; NIPWVDH; -.
DR   Proteomes; UP000008185; 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_1000064486"
SQ   SEQUENCE   414 AA;  47141 MW;  B0B2843A26B27F23 CRC64;
     MTQANLSETL FKPRFKHTET STLVRRFNRG SQPPMQSALD GKNVPHWYRM INRLMWIWRG
     VDPREILDVQ ARIVMSDAER TDDDLYDTVI GYRGGNWIYE WAKQAMDWQQ KACQEQDAMR
     SGRYWLHAST LYNIAAYPHL KGDELAEQAQ ALANRAYEEA AQRLPGSLRE MEFAVPGGSP
     VTAFLHMPKG DGPFPTVLMC GGLDAMQTDY YTLYERYFAP RGIAMLTLDM PSVGFSSKWK
     LTQDSSLLHQ HVLKALPNVP WVDHTRVAAF GFRFGANVAV RLAYLEAPRL KAVACLGPVV
     HALLSDPQRQ STVPEMYLDV LASRLGMHDA SDEALRVELN RYSLKVQGLL GRRCPTPMLS
     GFWKNDPFSP EEESRLITTS SSDGKLIEIP FNPVYRNFDH ALQEITDWIN HRLC