ID   YUAR_ECOLI              Reviewed;         499 AA.
AC   P34211;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 3.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Putative hydrolase YuaR;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   Name=yuaR; Synonyms=yddA; OrderedLocusNames=ECOK12F030;
OS   Escherichia coli (strain K12).
OG   Plasmid F.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / ATCC 12435 / DSM 5695 / NBRC 3302 / NCIMB 9481 / W1485;
RA   Henning U.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / CR63;
RA   Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
RT   "Complete nucleotide sequence of the F plasmid: its implications for
RT   organization and diversification of plasmid genomes.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-226.
RC   STRAIN=K12 / ATCC 12435 / DSM 5695 / NBRC 3302 / NCIMB 9481 / W1485;
RX   PubMed=8288530; DOI=10.1128/jb.176.2.359-367.1994;
RA   Kaufmann A., Stierhof Y.-D., Henning U.;
RT   "New outer membrane-associated protease of Escherichia coli K-12.";
RL   J. Bacteriol. 176:359-367(1994).
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; X74278; CAA52339.1; -; Genomic_DNA.
DR   EMBL; AP001918; BAA97900.1; -; Genomic_DNA.
DR   PIR; B36944; B36944.
DR   RefSeq; NP_061409.1; NC_002483.1.
DR   RefSeq; WP_010892530.1; NC_002483.1.
DR   AlphaFoldDB; P34211; -.
DR   SMR; P34211; -.
DR   ESTHER; ecoli-yuar; AlphaBeta_hydrolase.
DR   PRIDE; P34211; -.
DR   PhylomeDB; P34211; -.
DR   PRO; PR:P34211; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..499
FT                   /note="Putative hydrolase YuaR"
FT                   /id="PRO_0000027326"
FT   DOMAIN          94..393
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        207
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        460
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        418..499
FT                   /note="NTVLPSGLLFVAHKYDPTTPWINARKMADKFSAPLLTINGDGHTLALAGTNL
FT                   CVDEAVVRHLLFPGKSEDITCQGSGTGDTN -> ILFYHPVYCLWHTNMIRQLPG (in
FT                   Ref. 1; CAA52339)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   499 AA;  55682 MW;  B12589807134A26A CRC64;
     MRVIMKPLRR TLVFFIFSVF LCGTVSARQI EWQSCMTSPY SDWFGKESSS PELLCGYLSV
     PLKYTDTGKD VSDENIPLVR LAMTKLPAKS KRKGSVIIIS GGPGLPGINP YINFDWPVTN
     LRESWDIIGF DPRGVGQSFP AINCQQSNQE RLVNVSEKQL ILQKINACIH NTGAEVIRHI
     GSHEAVYDIE RIRQALGDKQ LTAVAYSYGT QIAALYAERF PSSIRSIVFD GVVDIDDLND
     NFSWKLRQAH SYQETFDRFA AWCARTKSCP LSSDRNQAIH QFHQLLLKLH NSPLTDSRGE
     SISSDDLISL TTELLLWRSS WPTLATAVRQ FSQGIVSNEI ETALNSSIAS EKVSDALGVI
     LCVDQSDEQL SQEQRKSRKK ALADAFPAVN FEREQSDLPE FCELWPIHRD LQQTRLKNTV
     LPSGLLFVAH KYDPTTPWIN ARKMADKFSA PLLTINGDGH TLALAGTNLC VDEAVVRHLL
     FPGKSEDITC QGSGTGDTN