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Database: UniProt
Entry: A0A1I0F2Q5_9BACI
LinkDB: A0A1I0F2Q5_9BACI
Original site: A0A1I0F2Q5_9BACI 
ID   A0A1I0F2Q5_9BACI        Unreviewed;       413 AA.
AC   A0A1I0F2Q5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Aminopeptidase II. Metallo peptidase. MEROPS family M29 {ECO:0000313|EMBL:SET52166.1};
GN   ORFNames=SAMN05216389_11394 {ECO:0000313|EMBL:SET52166.1};
OS   Oceanobacillus limi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=930131 {ECO:0000313|EMBL:SET52166.1, ECO:0000313|Proteomes:UP000198618};
RN   [1] {ECO:0000313|EMBL:SET52166.1, ECO:0000313|Proteomes:UP000198618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10780 {ECO:0000313|EMBL:SET52166.1,
RC   ECO:0000313|Proteomes:UP000198618};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOHE01000013; SET52166.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0F2Q5; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000198618; 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:SET52166.1}; 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:UP000198618}.
SQ   SEQUENCE   413 AA;  45897 MW;  14E921B0017E3A40 CRC64;
     MVSQQTQEKY AELALRTGVN LQKGQALMIN APLEGAEFTK MVVRKAYEIG AKDVHINWVD
     DELTLLKYEN APDEVIADYP EWKVKLHDRF AEDGAAVLNI RSTNPDLLKD IDPTRVAKAN
     KAAAQAMKNF RKYTMNDKIT WSIISIPTGD WAQKIFPDKS REDAIESLWD AIVKIVRVDQ
     EDPVAAWDEH NQTLITAREI LNEKNYKKLV FKAPGTELEM ELPEGHIWKG GSAVSEKGIT
     FNPNMPTEEV FSMPHKYGVN GTVSSTKPLN YGGSLIDNFS LTFKDGKVVD FKAEQGEGTL
     KHLLETDEGA KRLGEVALVP HESPVSQSGL IFYNTLFDEN ASCHIALGKA YPTNIKDGSG
     MSEEELDKHG VNDSLTHVDF MIGSEKLDID GVKADGTTEP VFRNGTWALD IKG
//
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