ID   SPRT_ECOSE              Reviewed;         165 AA.
AC   B6I782;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Protein SprT {ECO:0000255|HAMAP-Rule:MF_00746};
GN   Name=sprT {ECO:0000255|HAMAP-Rule:MF_00746}; OrderedLocusNames=ECSE_3212;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009240; BAG78736.1; -; Genomic_DNA.
DR   RefSeq; WP_000858396.1; NC_011415.1.
DR   AlphaFoldDB; B6I782; -.
DR   EnsemblBacteria; BAG78736; BAG78736; ECSE_3212.
DR   GeneID; 66673175; -.
DR   KEGG; ecy:ECSE_3212; -.
DR   HOGENOM; CLU_113336_0_1_6; -.
DR   OMA; QPHGEEW; -.
DR   Proteomes; UP000008199; 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_1000133240"
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