ID A0A0J6D2B5_9BACI Unreviewed; 417 AA.
AC A0A0J6D2B5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:KMM38439.1};
GN ORFNames=AB986_03840 {ECO:0000313|EMBL:KMM38439.1};
OS Alkalihalobacillus macyae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM38439.1, ECO:0000313|Proteomes:UP000035996};
RN [1] {ECO:0000313|EMBL:KMM38439.1, ECO:0000313|Proteomes:UP000035996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM38439.1,
RC ECO:0000313|Proteomes:UP000035996};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M29 family.
CC {ECO:0000256|ARBA:ARBA00008236}.
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:KMM38439.1}.
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DR EMBL; LELK01000001; KMM38439.1; -; Genomic_DNA.
DR RefSeq; WP_048309551.1; NZ_LELK01000001.1.
DR AlphaFoldDB; A0A0J6D2B5; -.
DR STRING; 157733.AB986_03840; -.
DR PATRIC; fig|157733.3.peg.2990; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000035996; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:KMM38439.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000035996}.
SQ SEQUENCE 417 AA; 46883 MW; 3A58710D7FEB6A5A CRC64;
MFKGIYEFIS EAQLKKYAKL AVGAGVNLQK NQLLIIHSDI QNATFARLIQ TIAYDAGASN
VFIDWTDEQS TKEFYLNAAD SVIDHFPDWQ AARFKEWDDA GAAYIHIISE NLEVFKEVST
ERINRFQKAS RTKLRDYYAK IRSHKVRWCL LAVPSVEWAT KVFPNLSIEE ALQSLWELIL
KGSRADGENP VKDWGIHNKA FESRKKILNE SQFESLHFTN RYGTDLSVGL PKNHLYIGGG
VIDKNGTPFF PNIPTEEIFT APHKHKVNGK LVGTKPLIYG GSVIDEFYLI FNNGRITDYY
AARGQEVLQN LIETDEGSHY LGEIALVSNK SPLAQADTLF FNTLFDENTS CHIGIGNASP
SNVQNGIEQS KEELKVSGLN TSLLLVNVTF GTEDMKVVGI KEGETEVLLL KDGDFQF
//
