ID   C0Z5L2_BREBN            Unreviewed;       368 AA.
AC   C0Z5L2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Aminopeptidase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=BBR47_51410 {ECO:0000313|EMBL:BAH46118.1};
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH46118.1, ECO:0000313|Proteomes:UP000001877};
RN   [1] {ECO:0000313|EMBL:BAH46118.1, ECO:0000313|Proteomes:UP000001877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599
RC   {ECO:0000313|Proteomes:UP000001877};
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) 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; AP008955; BAH46118.1; -; Genomic_DNA.
DR   RefSeq; WP_015893371.1; NC_012491.1.
DR   AlphaFoldDB; C0Z5L2; -.
DR   STRING; 358681.BBR47_51410; -.
DR   KEGG; bbe:BBR47_51410; -.
DR   eggNOG; COG2309; Bacteria.
DR   HOGENOM; CLU_057697_0_0_9; -.
DR   Proteomes; UP000001877; 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:SF1; BLL6088 PROTEIN; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   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:UP000001877}.
SQ   SEQUENCE   368 AA;  41567 MW;  4BC6DBC8603E7C6B CRC64;
     MLDPRLTKLA NVLVNYSTNV QPGDNVLIDA MEVDAALIKE LVKAVSRAGG HSFVNLRESS
     ISRQLLLAGT EEQFRLEAEM DKERMEKMQA CIIIEGGLNI NEMSDVPGEQ MKLATSFSKE
     VSIVRLKKKW VYLRYPTPSM AQLANKSTEA FEQFYFDVCT MDYAKMAKAM QPLKELMERT
     DRVKITGPGT ELTFSIKGIP AIPCPGQYNI PDGEVFTAPI RDSVNGVLSF NTPSPYQGFT
     FEKARLEFVD GKIVHATAND TERLNKILDT DEGARYIGEF ALGVNPFIRE PMQDILFDEK
     IDGSFHFTPG RCYDEASNGN MSNIHWDMVM IQRPEYGGGE IWFDDHLIRR DGRFLLPELE
     PLNPENLK
//