ID   SPRTL_STAAR             Reviewed;         151 AA.
AC   Q6GF11;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Protein SprT-like {ECO:0000255|HAMAP-Rule:MF_00745};
GN   OrderedLocusNames=SAR2150;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00745};
CC       Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00745};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00745}.
CC   -!- SIMILARITY: Belongs to the SprT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00745}.
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DR   EMBL; BX571856; CAG41131.1; -; Genomic_DNA.
DR   RefSeq; WP_001058376.1; NC_002952.2.
DR   AlphaFoldDB; Q6GF11; -.
DR   KEGG; sar:SAR2150; -.
DR   HOGENOM; CLU_123820_0_0_9; -.
DR   OMA; LVHYHLH; -.
DR   OrthoDB; 1262202at2; -.
DR   Proteomes; UP000000596; 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_00745; SprT_like; 1.
DR   InterPro; IPR006640; SprT-like_domain.
DR   InterPro; IPR035240; SprT_Zn_ribbon.
DR   InterPro; IPR023524; Uncharacterised_SprT-like.
DR   Pfam; PF10263; SprT-like; 1.
DR   Pfam; PF17283; Zn_ribbon_SprT; 1.
DR   SMART; SM00731; SprT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Zinc.
FT   CHAIN           1..151
FT                   /note="Protein SprT-like"
FT                   /id="PRO_0000213299"
FT   DOMAIN          6..147
FT                   /note="SprT-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00745"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00745"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00745"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00745"
SQ   SEQUENCE   151 AA;  18210 MW;  4F07F6898050D6F7 CRC64;
     MNNEILQRMV ENLSEEKFGR TFQHRAYFNK RLRTTGGRYL LKSHDIEINP KQYEHYGEDA
     VVKIILHELC HYHLHIAGKG YQHKDQDFKR LSQQVGAPRF CNSIESYQQR ANYEYYCTKC
     HAKYIRIRKV DTNRMRCGHC NGKLRMKRQL K