ID   Y1567_STAAB             Reviewed;         351 AA.
AC   Q2YTD2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Uncharacterized peptidase SAB1567;
DE            EC=3.4.-.-;
GN   OrderedLocusNames=SAB1567;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI81256.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ938182; CAI81256.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000161678.1; NC_007622.1.
DR   AlphaFoldDB; Q2YTD2; -.
DR   SMR; Q2YTD2; -.
DR   KEGG; sab:SAB1567; -.
DR   HOGENOM; CLU_017266_4_2_9; -.
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 SAB1567"
FT                   /id="PRO_0000299421"
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;  39624 MW;  ACFE3957192CD20F CRC64;
     MTKISKIIDE LNNQQADAAW ITTPLNVYYF TGYRSEPHER LFALLIKKDG KQVLFCPKME
     VEEVKASSFT GEIVGYLDTE NPFSLYPQTI NKLLIESEHL TVARQKQLIS GFNVNSFGDV
     DLTIKQLRNI KSEDEISKIR KAAELADKCI EIGVSYLKEG VTEREVVNHI EQTIKQYGVN
     EMSFDTMVLF GDHAASPHGT PGDRRLKSNE YVLFDLGVIY EHYCSDMTRT IKFGEPNKEA
     QEIYNIVLEA ETSAIQAIKP GIPLKDIDHI ARNIISEKGY GEYFPHRLGH GLGLQEHEYQ
     DVSSTNSNLL EAGMVITIEP GIYVPGVAGV RIEDDILVTN EGYEVLTHYE K