ID A0A139P262_9STRE Unreviewed; 360 AA.
AC A0A139P262;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Proline dipeptidase {ECO:0000313|EMBL:KXT82380.1};
DE EC=3.4.13.9 {ECO:0000313|EMBL:KXT82380.1};
GN ORFNames=STRDD11_01881 {ECO:0000313|EMBL:KXT82380.1};
OS Streptococcus sp. DD11.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777879 {ECO:0000313|EMBL:KXT82380.1, ECO:0000313|Proteomes:UP000070514};
RN [1] {ECO:0000313|EMBL:KXT82380.1, ECO:0000313|Proteomes:UP000070514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD11 {ECO:0000313|EMBL:KXT82380.1,
RC ECO:0000313|Proteomes:UP000070514};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
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 -!- 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:KXT82380.1}.
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DR EMBL; LQRF01000227; KXT82380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139P262; -.
DR STRING; 1777879.STRDD11_01881; -.
DR PATRIC; fig|1777879.3.peg.2090; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000070514; 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:KXT82380.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KXT82380.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:KXT82380.1}.
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; 40358 MW; 0276A43E34B7557C CRC64;
MTKINQITAY LEHEKTDAAV FSDPVSINYL TGFYSDPHER QMFLFVYPHQ EPLLFVPALE
ADRAASILDF QVVGYVDSEN PWQKIKNTLP AAPFRKIAVE FDHLILTKYH GLRTVFEGAE
FTNLTPLINR LRLIKSADEI QKMLIAGQYA DKAVNIGFDS ISLDKTETDI IAQIDFAIKR
EGYEMSFETM VLTGDNAANP HGIPGAHTIE NNALLLFDLG CMVNGYASDM TRTVAVGQPD
QFKKEIYQLT LEAQQAALDF IKPGVTAHEV DRAARQVIEK AGYGEYFNHR LGHGIGMDVH
EFPSIMEGND MVIEEGMCFS VEPGIYIPGK VGVRIEDCGH VTKNGFELFT ETSKDLLYFE
//
