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Database: UniProt
Entry: A0A0C5FYM9_9ACTN
LinkDB: A0A0C5FYM9_9ACTN
Original site: A0A0C5FYM9_9ACTN 
ID   A0A0C5FYM9_9ACTN        Unreviewed;       432 AA.
AC   A0A0C5FYM9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   ORFNames=TU94_16095 {ECO:0000313|EMBL:AJP02768.1};
OS   Streptomyces cyaneogriseus subsp. noncyanogenus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP02768.1, ECO:0000313|Proteomes:UP000032234};
RN   [1] {ECO:0000313|EMBL:AJP02768.1, ECO:0000313|Proteomes:UP000032234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP02768.1,
RC   ECO:0000313|Proteomes:UP000032234};
RA   Wang H., Li C., Xiang W., Wang X.;
RT   "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT   Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467,
CC       ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP010849; AJP02768.1; -; Genomic_DNA.
DR   RefSeq; WP_044382608.1; NZ_CP010849.1.
DR   AlphaFoldDB; A0A0C5FYM9; -.
DR   STRING; 477245.TU94_16095; -.
DR   KEGG; scw:TU94_16095; -.
DR   PATRIC; fig|477245.3.peg.3408; -.
DR   HOGENOM; CLU_019532_2_0_11; -.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000032234; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032234};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}.
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
SQ   SEQUENCE   432 AA;  45906 MW;  11B4C89664ECFD19 CRC64;
     MSAPSRFHHP HTDDLMAFLA ASPTPYHAVA NAAERLEKAG FRQVAETDAW DGTSGGKYVL
     RGGAIVAWYV PEGSAPHTPF RIVGAHTDSP NLRVKPLPDS GAHGWRQVAV EIYGGPLMNS
     WLDRDLGLAG RLTLRDGSTR LVDVDRPLLR VPQLAIHLDR TVSTEGLKLD KQRHLQPVWG
     LGDDVRDGDL VAFLEETAGI PAGEVTGWDL MTYPVEAPAY LGRDRELVAG PRMDNLLSVH
     AGTAALAAVA ASGGALPYIP VLAAFDHEEN GSQSDTGADG PLLGTVLERS VFARGGSYED
     RARAFAGTVC LSSDTGHAVH PNYAERHDPT HHPRVNGGPI LKVNVNNRYA TDGSGRAVFA
     AACEKAGVPF QSFVSHNSMP CGTTIGPITA ARHGIRTVDI GVAILSMHSA RELCGADDPY
     LLANALVAFL EG
//
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