ID Q8DT07_STRMU Unreviewed; 359 AA.
AC Q8DT07;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=Dipeptidase PepQ {ECO:0000313|EMBL:AAN59235.1};
GN Name=pepQ {ECO:0000313|EMBL:AAN59235.1};
GN OrderedLocusNames=SMU_1592 {ECO:0000313|EMBL:AAN59235.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN59235.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:AAN59235.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; AE014133; AAN59235.1; -; Genomic_DNA.
DR RefSeq; NP_721929.1; NC_004350.2.
DR RefSeq; WP_002262796.1; NC_004350.2.
DR AlphaFoldDB; Q8DT07; -.
DR STRING; 210007.SMU_1592; -.
DR MEROPS; M24.006; -.
DR DNASU; 1028824; -.
DR KEGG; smu:SMU_1592; -.
DR PATRIC; fig|210007.7.peg.1417; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_1_9; -.
DR OrthoDB; 9806388at2; -.
DR PhylomeDB; Q8DT07; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProt.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProt.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT DOMAIN 4..133
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 359 AA; 39811 MW; 0CF46BA0AF19D581 CRC64;
MSKLAQIVQK LKKQGIEAAV LSDPVSINYL TGFYSDPHER LMFLFLFADQ EPLLFLPELD
ALRAKSILDI SVTGYLDFEN PLEKIKTLLP KTNYSKIALE FDNLNVTKFK GLETIFSGQF
TNLTPLINRM RLIKSADEIQ KLLIAGELAD KAVQIGFDSI SLNATETDII AQIEFEMKKL
GVDKMSFETM VLTGSNAANP HGLPASHKIE NNHLLLFDLG VESTGYVSDM TRTVAVGQPD
QFKKDIYNIC LEAQLTALDF IKPGVSAAQV DAAARSVIEK AGYGDYFNHR LGHGIGMGLH
EFPSIMAGND MLLEEGMCFS VEPGIYIPEK VGVRIEDCGH VTKNGFEVFT QTPKELLYF
//
