ID   SPRT_ECO45              Reviewed;         165 AA.
AC   B7MMD2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Protein SprT {ECO:0000255|HAMAP-Rule:MF_00746};
GN   Name=sprT {ECO:0000255|HAMAP-Rule:MF_00746}; OrderedLocusNames=ECS88_3226;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
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; CU928161; CAR04461.1; -; Genomic_DNA.
DR   RefSeq; WP_000858396.1; NC_011742.1.
DR   AlphaFoldDB; B7MMD2; -.
DR   EnsemblBacteria; CAR04461; CAR04461; ECS88_3226.
DR   GeneID; 66673175; -.
DR   KEGG; ecz:ECS88_3226; -.
DR   HOGENOM; CLU_113336_0_1_6; -.
DR   OMA; QPHGEEW; -.
DR   Proteomes; UP000000747; Chromosome.
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_1000133235"
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;  19321 MW;  E414A39930CD91A9 CRC64;
     MKTSRLPIAI QQAVMRRLRE KLAQANLKLG RNYPEPKLSY TQRGTSAGTA WLESYEIRLN
     PVLLLENSEA FIEEVVPHEL AHLLVWKHFG RVAPHGKEWK WMMESVLGVP ARRTHQFELQ
     SVRRNTFPYR CKCQEHQLTV RRHNRVVRGE AVYRCVHCGE QLVAK