ID   C4L2F8_EXISA            Unreviewed;       412 AA.
AC   C4L2F8;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Peptidase M29 aminopeptidase II {ECO:0000313|EMBL:ACQ71210.1};
GN   OrderedLocusNames=EAT1b_2288 {ECO:0000313|EMBL:ACQ71210.1};
OS   Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ71210.1, ECO:0000313|Proteomes:UP000000716};
RN   [1] {ECO:0000313|EMBL:ACQ71210.1, ECO:0000313|Proteomes:UP000000716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX   PubMed=21460088; DOI=10.1128/JB.00303-11;
RA   Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA   Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA   Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA   Hendrix C., Richardson P., Tiedje J.M.;
RT   "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT   AT1b.";
RL   J. Bacteriol. 193:2880-2881(2011).
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; CP001615; ACQ71210.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4L2F8; -.
DR   STRING; 360911.EAT1b_2288; -.
DR   MEROPS; M29.002; -.
DR   KEGG; eat:EAT1b_2288; -.
DR   eggNOG; COG2309; Bacteria.
DR   HOGENOM; CLU_054346_1_0_9; -.
DR   Proteomes; UP000000716; Chromosome.
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:ACQ71210.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
SQ   SEQUENCE   412 AA;  45008 MW;  BE1ECB8EB9A20411 CRC64;
     MSKISMPTEA DFARYAELAV KKGVNIQPGQ QLEVRADISQ APLVRHVVKA AYAAGAKQVF
     VNWSDEETGK IRYFNAPADS FKEFPDWLKA RFEQLAEEKT AFLSIVSDDP DALNGVESSR
     ISDANRAAGQ ALAKWRQYVM SDNVSWSIVA GASEAWAQKV FPGRDDAVAA LWQAIFAATR
     MDQEDVVAAW DTHDQSLRSR AKLLTEKKYA KLHYKAPGTE LTIGLPKKHV FLGGGGPNVD
     GIDFIANMPT EEVFTLADKD SVEGHVSSTK PLSYSGNLID EFTLWFEGGK VVKAEAKKGQ
     AALDELLNMD EGARRIGEVA LVPDDSPISN SGLLFYNTLF DENASCHLAL GRAYSTCLEG
     GPSMSQEELA ANGANDSMTH VDFMIGSAEM NIDGEREDGT REAIMRDGNW VI
//