ID   A0A143X2B4_9FIRM        Unreviewed;       459 AA.
AC   A0A143X2B4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeA {ECO:0000313|EMBL:CVH76961.1};
GN   ORFNames=BN3662_01902 {ECO:0000313|EMBL:CVH76961.1};
OS   Clostridiales bacterium CHKCI006.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1780379 {ECO:0000313|EMBL:CVH76961.1, ECO:0000313|Proteomes:UP000198633};
RN   [1] {ECO:0000313|EMBL:CVH76961.1, ECO:0000313|Proteomes:UP000198633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHKC6 {ECO:0000313|EMBL:CVH76961.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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|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; FCNA01000099; CVH76961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143X2B4; -.
DR   STRING; 1780379.BN3662_01902; -.
DR   Proteomes; UP000198633; Unassembled WGS sequence.
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; cd05659; M18_API; 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:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 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:UP000198633};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   459 AA;  50895 MW;  FE11B16CF7E3843A CRC64;
     MMKKSAWYKY DEKALSDVFH FNDDYKAFLS ECKTERECTL SAVELAKKAG YMDLETCIQN
     NTSLKPGDKV YANNKDKNIA LFIIGEEPIE NGMNILGAHI DSPRIDLKQV PLYEDTEICL
     LDTHYYGGIK KYQWVALPLA MHGVVVKKDG TKVNVVIGED DNDPVLGISD LLPHLAQTQM
     KKDAGSIIEG EDLNVTFGSM PSKDEEKEAV KANIKKLLKE KYDIEEEDFI SAELEIVPAG
     KARDFGIDRS MVMGYGHDDR VCGYTSLRAI LDTDTVKKTA CCLLVDKEEV GSIGATGMQS
     KFFENTVAEL INLTGDYNDL KLRRALTNSY MLSSDVSAGY DPNYPAVMER KNSAYLGYGP
     AFNKYTGARG KSGCNDASPE FIASLRKTMD DANISWQTAE LGRVDQGGGG TIAYILANYN
     MQVIDCGVPV HNMHAPWEVC SKADIYEAYK GYLAFLKQA
//