ID   SPRT_PROMH              Reviewed;         168 AA.
AC   B4F1B5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Protein SprT {ECO:0000255|HAMAP-Rule:MF_00746};
GN   Name=sprT {ECO:0000255|HAMAP-Rule:MF_00746}; OrderedLocusNames=PMI2105;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(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}.
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DR   EMBL; AM942759; CAR44204.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4F1B5; -.
DR   EnsemblBacteria; CAR44204; CAR44204; PMI2105.
DR   KEGG; pmr:PMI2105; -.
DR   eggNOG; COG3091; Bacteria.
DR   HOGENOM; CLU_113336_0_1_6; -.
DR   Proteomes; UP000008319; 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; IPR023483; Uncharacterised_SprT.
DR   PANTHER; PTHR38773; PROTEIN SPRT; 1.
DR   PANTHER; PTHR38773:SF1; PROTEIN SPRT; 1.
DR   Pfam; PF10263; SprT-like; 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..168
FT                   /note="Protein SprT"
FT                   /id="PRO_1000133245"
FT   DOMAIN          20..166
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   168 AA;  19838 MW;  56666C9283A77B56 CRC64;
     MKTVRVPIAL VQSVMRTLRE KLQQANKYLN TDYPEPTLQY NQRGTIAGSA YYANWEIRLN
     PTLLIENKQN FIEEVIPHEL AHLLVSRHFG RVAPHGKEWK WMMETVLQVS AKRTHHFDIS
     NVTAKTFSYA CRCQEIHQLT LRRHNKVQRG ETQYRCRHCQ AILQLIKE
//