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Database: UniProt
Entry: A0A0Q3WW66_9BACI
LinkDB: A0A0Q3WW66_9BACI
Original site: A0A0Q3WW66_9BACI 
ID   A0A0Q3WW66_9BACI        Unreviewed;       365 AA.
AC   A0A0Q3WW66;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Metallopeptidase {ECO:0000313|EMBL:KQL53303.1};
GN   ORFNames=AN964_07240 {ECO:0000313|EMBL:KQL53303.1};
OS   Heyndrickxia shackletonii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL53303.1, ECO:0000313|Proteomes:UP000051888};
RN   [1] {ECO:0000313|EMBL:KQL53303.1, ECO:0000313|Proteomes:UP000051888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL53303.1,
RC   ECO:0000313|Proteomes:UP000051888};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-2015) 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:KQL53303.1}.
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DR   EMBL; LJJC01000004; KQL53303.1; -; Genomic_DNA.
DR   RefSeq; WP_055739031.1; NZ_LJJC01000004.1.
DR   AlphaFoldDB; A0A0Q3WW66; -.
DR   STRING; 157838.AN964_07240; -.
DR   PATRIC; fig|157838.3.peg.1595; -.
DR   OrthoDB; 9806388at2; -.
DR   Proteomes; UP000051888; 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:UP000051888}.
FT   DOMAIN          4..138
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          146..348
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
SQ   SEQUENCE   365 AA;  40864 MW;  82520E0B1A3A1F39 CRC64;
     MNQRLQSLTE WLKTENIDAA FITSSENVFY LSGFYSDPHE RLLGIAVFQD KEPFLICPAL
     DAHDAKQSGW EYEIIGCSDT DNAWDIVAQN MKSRVEKVAK MALEKEHINL ERYEEILKRF
     AGASFVAAEE KLRELRLVKD ENEKQILKKA AEYADFAVQV GINEIAEGKT ELDIIAAIEY
     ELKKKGISQM SFETMVLTGN NAASPHGNPG LTKIKKGDLV LFDLGVIYEG YCSDITRTVA
     YDHINDEQHK IYHTVLKAEE EAVKAVKPGI KAKELDQLAR DIITDAGYGE YFTHRLGHGL
     GIGVHEFPSV TNTNELVLKE GMVFTIEPGI YVPGIAGVRI EDDVFVTKNG VDVLTSFDKT
     LQIIK
//
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