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