ID FRSA_ECOLI Reviewed; 414 AA.
AC P04335; P77413;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Esterase FrsA {ECO:0000255|HAMAP-Rule:MF_01063, ECO:0000305};
DE EC=3.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01063, ECO:0000269|PubMed:15808744};
DE AltName: Full=Fermentation/respiration switch protein {ECO:0000303|PubMed:15169777};
GN Name=frsA {ECO:0000255|HAMAP-Rule:MF_01063, ECO:0000303|PubMed:15169777};
GN Synonyms=yafA; OrderedLocusNames=b0239, JW0229;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6397401; DOI=10.1016/0378-1119(84)90052-0;
RA Nueesch J., Schuemperli D.;
RT "Structural and functional organization of the gpt gene region of
RT Escherichia coli.";
RL Gene 32:243-249(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 242; 277-278 AND 397-414.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH IIAGLC,
RP OVEREXPRESSION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15169777; DOI=10.1074/jbc.m405048200;
RA Koo B.M., Yoon M.J., Lee C.R., Nam T.W., Choe Y.J., Jaffe H.,
RA Peterkofsky A., Seok Y.J.;
RT "A novel fermentation/respiration switch protein regulated by enzyme IIAGlc
RT in Escherichia coli.";
RL J. Biol. Chem. 279:31613-31621(2004).
RN [7]
RP FUNCTION AS AN ESTERASE, AND CATALYTIC ACTIVITY.
RX PubMed=15808744; DOI=10.1016/j.femsre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of esters (PubMed:15808744).
CC Displays esterase activity toward pNP-butyrate (PubMed:15808744). May
CC stimulate mixed-acid fermentation by acting as a
CC fermentation/respiration switch that down-regulates respiration and up-
CC regulates fermentation rates (PubMed:15169777).
CC {ECO:0000269|PubMed:15169777, ECO:0000269|PubMed:15808744}.
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 ECO:0000269|PubMed:15808744};
CC -!- SUBUNIT: Forms a 1:1 complex specifically with the unphosphorylated
CC form of the EIIA component of the glucose-specific PTS system (IIAGlc).
CC {ECO:0000269|PubMed:15169777}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene increases cell respiration
CC rate on several sugars including glucose.
CC {ECO:0000269|PubMed:15169777}.
CC -!- MISCELLANEOUS: Increased expression results in an increased
CC fermentation rate on sugars with the concomitant accumulation of mixed-
CC acid fermentation products. {ECO:0000269|PubMed:15169777}.
CC -!- SIMILARITY: Belongs to the FrsA family. {ECO:0000255|HAMAP-
CC Rule:MF_01063, ECO:0000305}.
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DR EMBL; M13422; AAA23929.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73343.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77908.2; -; Genomic_DNA.
DR EMBL; U70214; AAB08659.1; -; Genomic_DNA.
DR PIR; H64748; QQEC49.
DR RefSeq; NP_414774.1; NC_000913.3.
DR RefSeq; WP_000189532.1; NZ_SSZK01000050.1.
DR AlphaFoldDB; P04335; -.
DR SMR; P04335; -.
DR BioGRID; 4261742; 12.
DR BioGRID; 850400; 1.
DR DIP; DIP-11208N; -.
DR IntAct; P04335; 7.
DR STRING; 511145.b0239; -.
DR ESTHER; ecoli-yafa; Duf_1100-R.
DR jPOST; P04335; -.
DR PaxDb; 511145-b0239; -.
DR EnsemblBacteria; AAC73343; AAC73343; b0239.
DR GeneID; 946039; -.
DR KEGG; ecj:JW0229; -.
DR KEGG; eco:b0239; -.
DR PATRIC; fig|1411691.4.peg.2044; -.
DR EchoBASE; EB1083; -.
DR eggNOG; COG1073; Bacteria.
DR HOGENOM; CLU_036819_0_0_6; -.
DR InParanoid; P04335; -.
DR OMA; NIPWVDH; -.
DR OrthoDB; 5590073at2; -.
DR PhylomeDB; P04335; -.
DR BioCyc; EcoCyc:EG11091-MONOMER; -.
DR BRENDA; 3.1.1.1; 2026.
DR PRO; PR:P04335; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0106435; F:carboxylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IDA:EcoCyc.
DR GO; GO:0043470; P:regulation of carbohydrate catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..414
FT /note="Esterase FrsA"
FT /id="PRO_0000197151"
FT CONFLICT 242
FT /note="T -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..278
FT /note="NV -> TL (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 397..414
FT /note="NFDKGLQEITDWIEKRLC -> KILTKVFRKSPTGSKNACVKNLLNFANLVK
FT QLHHNRR (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 47009 MW; 2C154E46CFC9565E CRC64;
MTQANLSETL FKPRFKHPET STLVRRFNHG AQPPVQSALD GKTIPHWYRM INRLMWIWRG
IDPREILDVQ ARIVMSDAER TDDDLYDTVI GYRGGNWIYE WATQAMVWQQ KACAEDDPQL
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 GLQEITDWIE KRLC
//
