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Database: UniProt
Entry: A0A263BW48_9BACI
LinkDB: A0A263BW48_9BACI
Original site: A0A263BW48_9BACI 
ID   A0A263BW48_9BACI        Unreviewed;       371 AA.
AC   A0A263BW48;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Peptidase M24 family protein {ECO:0000313|EMBL:OZM57971.1};
GN   ORFNames=CIB95_06340 {ECO:0000313|EMBL:OZM57971.1};
OS   Lottiidibacillus patelloidae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lottiidibacillus.
OX   NCBI_TaxID=2670334 {ECO:0000313|EMBL:OZM57971.1, ECO:0000313|Proteomes:UP000217083};
RN   [1] {ECO:0000313|Proteomes:UP000217083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA5d-4 {ECO:0000313|Proteomes:UP000217083};
RA   Huang Z.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OZM57971.1, ECO:0000313|Proteomes:UP000217083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA5d-4 {ECO:0000313|EMBL:OZM57971.1,
RC   ECO:0000313|Proteomes:UP000217083};
RA   Liu R., Dong C., Shao Z.;
RT   "Bacillus patelloidae sp. nov., isolated from the intestinal tract of a
RT   marine limpet.";
RL   Submitted (SEP-2017) 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:OZM57971.1}.
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DR   EMBL; NPIA01000002; OZM57971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A263BW48; -.
DR   Proteomes; UP000217083; Unassembled WGS sequence.
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:UP000217083}.
FT   DOMAIN          10..144
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          152..354
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
SQ   SEQUENCE   371 AA;  41584 MW;  333D3B42F28B8D0A CRC64;
     MKGFVSLHTR IQQYTKWLND KNIDFSFITS TPNVFYLSKF YSNPHERLLG IGIFANEEPF
     LVCPKMEVGQ ARAAGWDFEI IGYSDTENPW QFMQESIQKR NVTVNSCAIE SSHLTYERSE
     QLRHILGGAT FISAEEKLHY MRMVKDDQEI SILREAAKLA DFGVEVGVSA LASGKTEMEV
     LAQIEFELKK KGIREMSFST MVLYGEKSAD PHGNPGLKKL ANGDFVLFDL GVVLDGYCSD
     ITRTVAYGDV SDKQKEIYNT VLKAEVSALE ACKIGTRIGD LDKIARGIIT EAGYGEYFPH
     RLGHGLGIDV HEFPSMNETN NDLLQEGMTF TIEPGIYVPS VGGVRIEDDV LITKDGYESL
     TQFPKELQII K
//
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