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SPRTL_STAAS
ID   SPRTL_STAAS             Reviewed;         151 AA.
AC   Q6G7P7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Protein SprT-like {ECO:0000255|HAMAP-Rule:MF_00745};
GN   OrderedLocusNames=SAS1967;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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; BX571857; CAG43774.1; -; Genomic_DNA.
DR   RefSeq; WP_001058111.1; NC_002953.3.
DR   AlphaFoldDB; Q6G7P7; -.
DR   KEGG; sas:SAS1967; -.
DR   HOGENOM; CLU_123820_0_0_9; -.
DR   OMA; LVHYHLH; -.
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_0000213300"
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;  18186 MW;  5689C7DE9036E4E7 CRC64;
     MNNDKLQRMV ENLSEEKFGR TFRHCAYFNK RLRTTGGRYL LKSHDIEINP KQYEHYGEDA
     VVKIILHELC HYHLHIAGKG YQHKDQDFKR LSQQVGAPRF CNSIESYQQR ANYEYYCTKC
     HAKYIRIRKV DTNRMRCGHC NGKLRMKRQL K
 
 
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