ID A0A160F7P1_9BACI Unreviewed; 364 AA.
AC A0A160F7P1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Metallopeptidase M24 family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GFC30_3067 {ECO:0000313|EMBL:ANB62302.1};
OS Anoxybacillus amylolyticus.
OG Plasmid pdsm15939_1 {ECO:0000313|Proteomes:UP000076865}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB62302.1, ECO:0000313|Proteomes:UP000076865};
RN [1] {ECO:0000313|EMBL:ANB62302.1, ECO:0000313|Proteomes:UP000076865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB62302.1,
RC ECO:0000313|Proteomes:UP000076865};
RC PLASMID=Plasmid pdsm15939_1 {ECO:0000313|Proteomes:UP000076865};
RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA Gambacorta A., Nicolaus B.;
RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT bacterium isolated from Mount Rittmann (Antarctica).";
RL Syst. Appl. Microbiol. 29:300-307(2006).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; CP015439; ANB62302.1; -; Genomic_DNA.
DR RefSeq; WP_066327649.1; NZ_CP015439.1.
DR AlphaFoldDB; A0A160F7P1; -.
DR KEGG; aamy:GFC30_3067; -.
DR PATRIC; fig|294699.3.peg.3171; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000076865; Plasmid pdsm15939_1.
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 Plasmid {ECO:0000313|EMBL:ANB62302.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076865}.
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 364 AA; 40554 MW; 70DE65AEFC713BA6 CRC64;
MNQRLRAFSE WLQEQHITFA LITSTPNVFY LSGFYSDPHE RLLALLVFPN EEPVLVCPQM
EVEQAKHSGW AYSLIGYSDT DHPWELIANY LKKLALPIEK VAVEKSHLSL ERYEQFSTYF
PTRAMVNAEE KLRQLRMIKE ESEIAILRQA AALANLGVEV GIQTIAEGKT ELDIIATIEH
ELKKKGVREM SFATMVLTGE KTAAPHGVPG LTPIQRGDFV LFDLGVVLDG YCSDITRTVV
FGTPNEEQKR IYETVRKAQL AAIAASKPGA AVGTVDQAAR QIIEEAGYGP YFTHRVGHGL
GIEIHEYPCM NATNPLPLQR GMVFTIEPGI YVPSIGGVRI EDDVLITDTG VEVLTNYPKE
LIIL
//
