ID   A0A3R9NZC9_9BACI        Unreviewed;       410 AA.
AC   A0A3R9NZC9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   03-MAY-2023, entry version 11.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:RSL29480.1};
GN   ORFNames=D7Z54_30880 {ECO:0000313|EMBL:RSL29480.1};
OS   Salibacterium salarium.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX   NCBI_TaxID=284579 {ECO:0000313|EMBL:RSL29480.1, ECO:0000313|Proteomes:UP000275076};
RN   [1] {ECO:0000313|EMBL:RSL29480.1, ECO:0000313|Proteomes:UP000275076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IM0101 {ECO:0000313|EMBL:RSL29480.1,
RC   ECO:0000313|Proteomes:UP000275076};
RA   Yamprayoonswat W., Boonvisut S., Jumpathong W., Sittihan S., Ruangsuj P.,
RA   Wanthongcharoen S., Thongpramul N., Pimmason S., Yu B., Yasawong M.;
RT   "Draft genome sequence of Bacillus salarius IM0101, isolated from a
RT   hypersaline soil in Inner Mongolia, China.";
RL   Submitted (OCT-2018) 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:RSL29480.1}.
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DR   EMBL; RBVX01000064; RSL29480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R9NZC9; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000275076; 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:RSL29480.1}; 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:UP000275076}.
SQ   SEQUENCE   410 AA;  45429 MW;  E71050573059043A CRC64;
     MSHFDEKFNN YASLAIKKGV NIQEGQTLFI SAPITSSEFV RTLAEKAYDA GAKNVYVDWV
     DEQLTRLKYD KAPDEAFKEF PSWVARGREE LAENGAAFIT VKSTDPDLLK GVDSKRVADA
     NKAAGNAMDT FRSYIQSDMV SWLVIATPSP GWAKKVFPDD TQEEAENKLW DAIFKAVRAD
     VKDPVAEWEE HDKKLQEKAS FLNSKRFKEL HYKAPGTDLA ITLPEQHTWV GGGSPNKDGV
     HFIANMPTEE VFTVPHKTGV NGYVTNTKPL NYSGNIIDDF TIHFKDGKIT DYQAGEGEET
     LKNLIETDEG SHYLGEVALV PHSSPISQSG DLFYNTLFDE NASNHLAIGS AYAFCLENGA
     NMSKEEIQQH GLNNSITHVD FMVGSGDMDI DGVLADGTEE PIMRNGEWAV
//