Y1651_STAAW
ID Y1651_STAAW Reviewed; 351 AA.
AC Q8NW55;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Uncharacterized peptidase MW1651;
DE EC=3.4.-.-;
GN OrderedLocusNames=MW1651;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB95516.1; -; Genomic_DNA.
DR RefSeq; WP_000161667.1; NC_003923.1.
DR AlphaFoldDB; Q8NW55; -.
DR SMR; Q8NW55; -.
DR EnsemblBacteria; BAB95516; BAB95516; BAB95516.
DR KEGG; sam:MW1651; -.
DR HOGENOM; CLU_017266_4_2_9; -.
DR OMA; IHEWPYL; -.
DR Proteomes; UP000000418; 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 MW1651"
FT /id="PRO_0000299427"
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; 39637 MW; FF0B9E9187663663 CRC64;
MTKISKIIDE LNNQQADAAW ITTPLNVYYF TGYRSEPHER LFALLIKKDG KQVLFCPKME
VEEVKASPFT GEIVGYLDTE NPFSLYPQTI NKLLIESEHL TVARQKQLIS GFNVNSFGDV
DLTIKQLRNI KSEDEISKIR KAAELADKCI EIGVSYLKEG VTEREVVNHI EQTIKQYGVN
EMSFDTMVLF GDHAASPHGT PGDRRLKSNE YVLFDLGVIY EHYCSDMTRT IKFGEPSKEA
QEIYNIVLEA ETSAIQAIKP GIPLKDIDHI ARNIISEKGY GEYFPHRLGH GLGLQEHEYQ
DVSSTNSNLL EAGMVITIEP GIYVPSVAGV RIEDDILVTN EGYEVLTHYE K