ID   SPRT_KLEP7              Reviewed;         166 AA.
AC   A6TDV3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Protein SprT {ECO:0000255|HAMAP-Rule:MF_00746};
GN   Name=sprT {ECO:0000255|HAMAP-Rule:MF_00746};
GN   OrderedLocusNames=KPN78578_33130; ORFNames=KPN_03377;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR78774.1; -; Genomic_DNA.
DR   RefSeq; WP_002916588.1; NC_009648.1.
DR   AlphaFoldDB; A6TDV3; -.
DR   STRING; 272620.KPN_03377; -.
DR   PaxDb; 272620-KPN_03377; -.
DR   EnsemblBacteria; ABR78774; ABR78774; KPN_03377.
DR   KEGG; kpn:KPN_03377; -.
DR   HOGENOM; CLU_113336_0_1_6; -.
DR   Proteomes; UP000000265; 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   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   HAMAP; MF_00746; SprT; 1.
DR   InterPro; IPR006640; SprT-like_domain.
DR   InterPro; IPR035240; SprT_Zn_ribbon.
DR   InterPro; IPR023483; Uncharacterised_SprT.
DR   PANTHER; PTHR38773; PROTEIN SPRT; 1.
DR   PANTHER; PTHR38773:SF1; PROTEIN SPRT; 1.
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..166
FT                   /note="Protein SprT"
FT                   /id="PRO_1000046529"
FT   DOMAIN          20..164
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   166 AA;  19596 MW;  C8CED62056BDA8F4 CRC64;
     MKTPRIPIAI QQAVMRSLRE HLANANRKLE RRYAEPTLVY QQRGTSAGTA WLEKNEIRLN
     PVLLLENQRE FIDEVVPHEL AHLLVWQHFG RVAPHGKEWK WMMESVLGVP ARRTHRFELA
     SVRQNTFPYR CRCQQHQLTV RRHNRVVRGE ATYRCVRCGD LLVAEK
//