ID   X5DJM6_9CORY            Unreviewed;       454 AA.
AC   X5DJM6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeB {ECO:0000313|EMBL:AHW63283.1};
GN   ORFNames=CGLY_04175 {ECO:0000313|EMBL:AHW63283.1};
OS   Corynebacterium glyciniphilum AJ 3170.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW63283.1, ECO:0000313|Proteomes:UP000023703};
RN   [1] {ECO:0000313|EMBL:AHW63283.1, ECO:0000313|Proteomes:UP000023703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW63283.1};
RX   PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA   Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA   Ruckert C.;
RT   "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT   nov., nom. rev., isolated from putrefied banana.";
RL   Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP006842; AHW63283.1; -; Genomic_DNA.
DR   AlphaFoldDB; X5DJM6; -.
DR   STRING; 1404245.CGLY_04175; -.
DR   KEGG; cgy:CGLY_04175; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_11; -.
DR   Proteomes; UP000023703; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   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,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023703};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   454 AA;  47487 MW;  834A615EF81EF8F8 CRC64;
     MPEKQPEVSV PDAVRVRPGG LLVPMTDSTG PADFIDFIDA SPSSYHAAAE VASRLDAAGF
     ARQDEKAPWD ASPGGHYIVR GGAVLAWRIP EPAGERERPQ GFRIVGSHTD SPGLKLKPVG
     DITGPGGWRQ AAVEVYGGAI LPAWLDRELR LAGRVVLADG TEHLVCTGPV LRVPHLAIHL
     DRAVNNGLTL DRQQHMQPVF AVGEGAPTIG EVIADALSVE GVTPGDILAH DLITVDAQRG
     EVFGAQDDFI AAGRMDNLSS VFTSLQAFLA AGTDDATGGI IPVLAAFDHE EVGSATTSGA
     AGPVLEDVLT RTAAALGAGA EETRAMFARS SCVSADAAHS IHPNYAGKHD PVHRPVINGG
     PVLKVNANQR YASDATTSAA WRAACRSVGA PDQVFAGNND VPCGSTIGPI TATRLGIPTV
     DVGIPLLSMH SAREMAGVHD LAWFTDTLRA WWEQ
//