ID   SPRT_ECO8A              Reviewed;         165 AA.
AC   B7LYX4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Protein SprT {ECO:0000255|HAMAP-Rule:MF_00746};
GN   Name=sprT {ECO:0000255|HAMAP-Rule:MF_00746}; OrderedLocusNames=ECIAI1_3077;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00746};
CC       Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00746};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00746}.
CC   -!- SIMILARITY: Belongs to the SprT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00746}.
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DR   EMBL; CU928160; CAQ99892.1; -; Genomic_DNA.
DR   RefSeq; WP_001495390.1; NC_011741.1.
DR   AlphaFoldDB; B7LYX4; -.
DR   KEGG; ecr:ECIAI1_3077; -.
DR   HOGENOM; CLU_113336_0_1_6; -.
DR   OMA; QPHGEEW; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   HAMAP; MF_00746; SprT; 1.
DR   InterPro; IPR006640; SprT-like_domain.
DR   InterPro; IPR035240; SprT_Zn_ribbon.
DR   InterPro; IPR023483; Uncharacterised_SprT.
DR   Pfam; PF10263; SprT-like; 1.
DR   Pfam; PF17283; Zn_ribbon_SprT; 1.
DR   SMART; SM00731; SprT; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Zinc.
FT   CHAIN           1..165
FT                   /note="Protein SprT"
FT                   /id="PRO_1000133237"
FT   DOMAIN          20..163
FT                   /note="SprT-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00746"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00746"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00746"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00746"
SQ   SEQUENCE   165 AA;  19351 MW;  0A1513992BCC2AA9 CRC64;
     MKTSRLPIAI QQAVMRRLRE KLTQANLKLG RNYPEPKLSY TQRGTSAGTA WLESYEIRLN
     PVLLLENSEA FIEEVVPHEL AHLLVWKHFG RVAPHGKEWK WMMESVLGVP ARRTHQFELQ
     SVRRNTFPYR CKCQEHQLTV RRHNRVVRGE AVYRCVHCGE QLVAK