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Database: UniProt
Entry: A0A133Q2K1_STALU
LinkDB: A0A133Q2K1_STALU
Original site: A0A133Q2K1_STALU 
ID   A0A133Q2K1_STALU        Unreviewed;       351 AA.
AC   A0A133Q2K1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Putative Xaa-Pro dipeptidase {ECO:0000313|EMBL:KXA37100.1};
GN   ORFNames=HMPREF3225_02054 {ECO:0000313|EMBL:KXA37100.1};
OS   Staphylococcus lugdunensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=28035 {ECO:0000313|EMBL:KXA37100.1, ECO:0000313|Proteomes:UP000070063};
RN   [1] {ECO:0000313|EMBL:KXA37100.1, ECO:0000313|Proteomes:UP000070063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJR7738 {ECO:0000313|EMBL:KXA37100.1,
RC   ECO:0000313|Proteomes:UP000070063};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|RuleBase:RU000590}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXA37100.1}.
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DR   EMBL; LRQI01000079; KXA37100.1; -; Genomic_DNA.
DR   RefSeq; WP_002458866.1; NZ_KQ957392.1.
DR   AlphaFoldDB; A0A133Q2K1; -.
DR   STRING; 28035.B6N84_05865; -.
DR   PATRIC; fig|28035.7.peg.2078; -.
DR   eggNOG; COG0006; Bacteria.
DR   OMA; VGRTERH; -.
DR   Proteomes; UP000070063; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01092; APP-like; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 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   PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR46112:SF10; DIPEPTIDASE YKVY-RELATED; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000590}.
FT   DOMAIN          7..130
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          137..340
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
SQ   SEQUENCE   351 AA;  39737 MW;  59698F8223585D3B CRC64;
     MTNTDTIIET LKDQQADAAW ITTPLNIFYF TGYRSEPHER LFALLIKKNG EQILYCPKME
     VEEVKASPFE GKIIGYLDTE NPFNLMTQTF NKMLIESEHL TVKRQRELAQ GFNVKSFDDI
     DFTIKQLRNI KSASEIENIK KAAQLADKCI EIGVSFLRVG VKERDVVNHI ENEIKKYGVS
     EMSFDTMVLF GDHAASPHGT PGDRELQDNE YVLFDLGVIV NHYCSDMTRT VKFGTPENQA
     QEIYDIVLKA ETTAIKAIKP GVKLKAIDKI ARDIISEAGY GEYFPHRLGH GLGLEEHEYQ
     DVSSTNENVL EAGMVITIEP GIYVPNVAGV RIEDDILVTE NGYEILTRYD K
//
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