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Database: UniProt
Entry: I2J0F8_9STRE
LinkDB: I2J0F8_9STRE
Original site: I2J0F8_9STRE 
ID   I2J0F8_9STRE            Unreviewed;       360 AA.
AC   I2J0F8;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Xaa-Pro dipeptidase {ECO:0000313|EMBL:EIF36460.1};
DE            EC=3.4.13.9 {ECO:0000313|EMBL:EIF36460.1};
GN   ORFNames=HMPREF1117_0835 {ECO:0000313|EMBL:EIF36460.1};
OS   Streptococcus sp. SK643.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1095727 {ECO:0000313|EMBL:EIF36460.1, ECO:0000313|Proteomes:UP000006010};
RN   [1] {ECO:0000313|EMBL:EIF36460.1, ECO:0000313|Proteomes:UP000006010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK643 {ECO:0000313|EMBL:EIF36460.1,
RC   ECO:0000313|Proteomes:UP000006010};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:EIF36460.1}.
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DR   EMBL; AJMM01000026; EIF36460.1; -; Genomic_DNA.
DR   RefSeq; WP_000040948.1; NZ_AJMM01000026.1.
DR   AlphaFoldDB; I2J0F8; -.
DR   STRING; 1095727.HMPREF1117_0835; -.
DR   MEROPS; M24.006; -.
DR   PATRIC; fig|1095727.3.peg.1460; -.
DR   eggNOG; COG0006; Bacteria.
DR   OrthoDB; 9806388at2; -.
DR   Proteomes; UP000006010; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProt.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProt.
DR   GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
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; IPR001714; Pept_M24_MAP.
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   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   4: Predicted;
KW   Dipeptidase {ECO:0000313|EMBL:EIF36460.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EIF36460.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000313|EMBL:EIF36460.1}.
FT   DOMAIN          4..134
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          142..343
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
SQ   SEQUENCE   360 AA;  40308 MW;  628DBAEDA01E6A30 CRC64;
     MSKLQQIVTY LETEKLDVAV VSDPVTINYL TGFYSDPHER QMFLFVLADQ EPLLFVPALE
     VERATSTVSF PVVGYVDSEN PWQKMKHALP QLDFKRVAVE FDNLILTKYH GLKIVFETAE
     FENLTPRIQR MRLIKSADEV QKMMVAGLYA DKAVNVGFDN ISLDKTETDI IAQIDFAMKR
     EGYEMSFDTM VLTGDNAANP HGIPAANKVE NDALLLFDLG VLVNGYASDM TRTVAVGKPD
     QFKKDIYNLT LEAQQAALDF IKPGVTAHEV DRAAREVIEK AGYGEYFNHR LGHGIGMDVH
     EFPSIMEGND MVIEEGMCFS VEPGIYIPGK VGVRIEDCGV VTKDGFDLFT STSKDLLYFD
//
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