ID B9IVV2_BACCQ Unreviewed; 356 AA.
AC B9IVV2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Proline dipeptidase {ECO:0000313|EMBL:ACM14089.1};
GN Name=pepQ {ECO:0000313|EMBL:ACM14089.1};
GN OrderedLocusNames=BCQ_3661 {ECO:0000313|EMBL:ACM14089.1};
OS Bacillus cereus (strain Q1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM14089.1, ECO:0000313|Proteomes:UP000000441};
RN [1] {ECO:0000313|EMBL:ACM14089.1, ECO:0000313|Proteomes:UP000000441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1 {ECO:0000313|EMBL:ACM14089.1,
RC ECO:0000313|Proteomes:UP000000441};
RX PubMed=19060151; DOI=10.1128/JB.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
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DR EMBL; CP000227; ACM14089.1; -; Genomic_DNA.
DR AlphaFoldDB; B9IVV2; -.
DR MEROPS; M24.008; -.
DR KEGG; bcq:BCQ_3661; -.
DR HOGENOM; CLU_017266_4_2_9; -.
DR Proteomes; UP000000441; 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:SF3; AMINOPEPTIDASE YPDF; 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}.
FT DOMAIN 5..128
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 135..338
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 356 AA; 39907 MW; 2F7D8B5673A7CB42 CRC64;
MTLKMNKIQN QLQNYEIDGL LITKKENRQY ATGFTGSAGA VLISADKAVF ITDFRYVDQA
KSQIKDAEII MHKGNLEEEV ANQVSKLNIQ KLGIEENNMT LQQYKNLQKY VQAEMIQVCE
IIENIRIIKD TPEIETMKIA ANIADEAFHH ILTFLKPGIS ENTVRDELEF FMRKKGAASS
SFQIIVASGV RSSLPHGVAS NKIIERGDIV TLDFGALYDG YCSDITRTVV IGEPSEEFKK
IYNIVLEALK RGTEAIKPGE TAKRIDDITR NYITEHGYGQ YFGHSTGHGL GLEIHEPLRL
SQESKATLEE GMVVTVEPGI YIPNWGGCRI EDDIVITKDG YEVITKSNRE LIVIPC
//
