ID   SSNA_ECOLI              Reviewed;         442 AA.
AC   Q46812; Q2M9W1; Q47560;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Putative aminohydrolase SsnA;
DE            EC=3.-.-.-;
GN   Name=ssnA; Synonyms=ygfL; OrderedLocusNames=b2879, JW2847;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7764507; DOI=10.1271/bbb.58.117;
RA   Talukder A.A., Yanai S., Yamada M.;
RT   "Analysis of products of the Escherichia coli genomic genes and regulation
RT   of their expressions: an applicable procedure for genomic analysis of other
RT   microorganisms.";
RL   Biosci. Biotechnol. Biochem. 58:117-120(1994).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   [4]
RP   PROTEIN SEQUENCE OF 1-9.
RX   PubMed=10074077; DOI=10.1128/jb.181.6.1838-1846.1999;
RA   Yamada M., Talukder A.A., Nitta T.;
RT   "Characterization of the ssnA gene, which is involved in the decline of
RT   cell viability at the beginning of stationary phase in Escherichia coli.";
RL   J. Bacteriol. 181:1838-1846(1999).
CC   -!- INDUCTION: In stationary phase.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ATZ/TRZ family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA83060.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U28375; AAA83060.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC75917.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76945.1; -; Genomic_DNA.
DR   EMBL; D21141; BAA04677.1; -; Genomic_DNA.
DR   PIR; G65071; G65071.
DR   RefSeq; NP_417355.4; NC_000913.3.
DR   RefSeq; WP_000906252.1; NZ_LN832404.1.
DR   AlphaFoldDB; Q46812; -.
DR   SMR; Q46812; -.
DR   BioGRID; 4262326; 69.
DR   DIP; DIP-10923N; -.
DR   IntAct; Q46812; 4.
DR   STRING; 511145.b2879; -.
DR   PaxDb; Q46812; -.
DR   PRIDE; Q46812; -.
DR   DNASU; 949072; -.
DR   EnsemblBacteria; AAC75917; AAC75917; b2879.
DR   EnsemblBacteria; BAE76945; BAE76945; BAE76945.
DR   GeneID; 949072; -.
DR   KEGG; ecj:JW2847; -.
DR   KEGG; eco:b2879; -.
DR   PATRIC; fig|1411691.4.peg.3855; -.
DR   EchoBASE; EB2874; -.
DR   eggNOG; COG0402; Bacteria.
DR   HOGENOM; CLU_012358_2_6_6; -.
DR   InParanoid; Q46812; -.
DR   OMA; CYEVSDR; -.
DR   PhylomeDB; Q46812; -.
DR   BioCyc; EcoCyc:G7498-MON; -.
DR   PRO; PR:Q46812; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:CACAO.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR017700; Aminohydrolase_SsnA.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR03314; Se_ssnA; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Reference proteome;
KW   Zinc.
FT   CHAIN           1..442
FT                   /note="Putative aminohydrolase SsnA"
FT                   /id="PRO_0000122303"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   442 AA;  48842 MW;  2F6B45D8BF475C45 CRC64;
     MLILKNVTAV QLHPAKVQEG VDIAIENDVI VAIGDALTQR YPDASFKEMH GRIVMPGIVC
     SHNHFYSGLS RGIMANIAPC PDFISTLKNL WWRLDRALDE ESLYYSGLIC SLEAIKSGCT
     SVIDHHASPA YIGGSLSTLR DAFLKVGLRA MTCFETTDRN NGIKELQEGV EENIRFARLI
     DEAKKATSEP YLVEAHIGAH APFTVPDAGL EMLREAVKAT GRGLHIHAAE DLYDVSYSHH
     WYGKDLLARL AQFDLIDSKT LVAHGLYLSK DDITLLNQRD AFLVHNARSN MNNHVGYNHH
     LSDIRNLALG TDGIGSDMFE EMKFAFFKHR DAGGPLWPDS FAKALTNGNE LMSRNFGAKF
     GLLEAGYKAD LTICDYNSPT PLLADNIAGH IAFGMGSGSV HSVMVNGVMV YEDRQFNFDC
     DSIYAQARKA AASMWRRMDA LA