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Y1217_STAHJ
ID   Y1217_STAHJ             Reviewed;         351 AA.
AC   Q4L749;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Uncharacterized peptidase SH1217;
DE            EC=3.4.-.-;
GN   OrderedLocusNames=SH1217;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR   EMBL; AP006716; BAE04526.1; -; Genomic_DNA.
DR   RefSeq; WP_011275516.1; NC_007168.1.
DR   AlphaFoldDB; Q4L749; -.
DR   SMR; Q4L749; -.
DR   STRING; 279808.SH1217; -.
DR   EnsemblBacteria; BAE04526; BAE04526; SH1217.
DR   GeneID; 58062584; -.
DR   KEGG; sha:SH1217; -.
DR   eggNOG; COG0006; Bacteria.
DR   HOGENOM; CLU_017266_4_2_9; -.
DR   OMA; NENCAVE; -.
DR   OrthoDB; 415910at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF53092; SSF53092; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Metal-binding.
FT   CHAIN           1..351
FT                   /note="Uncharacterized peptidase SH1217"
FT                   /id="PRO_0000299430"
FT   BINDING         215
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         226
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         226
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         290
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         319
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         333
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         333
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   351 AA;  39777 MW;  9FBF4EE9E385BA75 CRC64;
     MSKIEKITKQ LQHEQADAAW ITTPLNVFYF TGYRSEPHER LFALLITANG DQTLYCPKME
     VEEVKNSPFE GKIIGYLDTE NPFEIDPLSF NKLLIESEHL TVKRQRELTQ NFGVQHYGDI
     DQTIKELRNI KNESEIENIR EAAKLADKCI EIGTEFLKVG VTEREVVNHI ENEIKKFGVS
     EMSFDTMVLF GDHAASPHGT PGERKLVKDE YVLFDLGVIY NHYCSDMTRT VKFGTPSEEA
     QTIYNIVLEA ETNAIEAIRA GVPLQDIDKI ARDIISDAGY GDYFPHRLGH GLGLEEHEYQ
     DVSSTNSNLL EAGMVITIEP GIYVPNVAGV RIEDDILVTE NGYEILTHYD K
 
 
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