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