ID   A0A1M6LEF8_9CLOT        Unreviewed;       468 AA.
AC   A0A1M6LEF8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=SAMN02745248_00730 {ECO:0000313|EMBL:SHJ69584.1};
OS   Hathewaya proteolytica DSM 3090.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hathewaya.
OX   NCBI_TaxID=1121331 {ECO:0000313|EMBL:SHJ69584.1, ECO:0000313|Proteomes:UP000183952};
RN   [1] {ECO:0000313|EMBL:SHJ69584.1, ECO:0000313|Proteomes:UP000183952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3090 {ECO:0000313|EMBL:SHJ69584.1,
RC   ECO:0000313|Proteomes:UP000183952};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FRAD01000005; SHJ69584.1; -; Genomic_DNA.
DR   RefSeq; WP_072902460.1; NZ_FRAD01000005.1.
DR   AlphaFoldDB; A0A1M6LEF8; -.
DR   STRING; 1121331.SAMN02745248_00730; -.
DR   OrthoDB; 89722at2; -.
DR   Proteomes; UP000183952; 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:UP000183952};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   468 AA;  52164 MW;  1DC2AE6C7E6E30C7 CRC64;
     MEQLDLKRKF STAWEKYDSK ELDEVMALSQ RYIDFMSLCK TERECVDEFV IRAEKNGYKN
     LTEIISHGNS IKAGDKIYVN HMGKALAMFL IGTEPIESGL RILGAHIDSP RLDLKQNPLF
     EEAELAYLKT HYYGGIKKYQ WLTLPLAIHG VFVKKDGTVT KVVFGEEENE PVVGISDLLV
     HLAGSQMEKT LGKAIEGEQL NVMVGSIPVE DKDLKERVKL NILNILNKKY GITEADFVSA
     EIEIVPAGRA KHFGLDNSMV LAYGHDDRIC SYTSFEAMLN IEQCDKTCVT LLVDKEEVGS
     IGATGMHSRF FENALAEIIN LKESNYTDLK VRRTLANSKM LSSDVSAAFD PSFADAFEKN
     NSAYFGRGIV FNKYTGSRGK SGCNDANAEY LAQLRNILDR NNVAWQTAEL GKVDQGGGGT
     IAYILAQYGM DVIDSGVALH SMHAPYELAS KADIYETCRA YEVFLKEI
//