ID   A0A1V4J0M5_9CLOT        Unreviewed;       441 AA.
AC   A0A1V4J0M5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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:OPJ65871.1};
GN   ORFNames=CLCHR_04440 {ECO:0000313|EMBL:OPJ65871.1};
OS   Clostridium chromiireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=225345 {ECO:0000313|EMBL:OPJ65871.1, ECO:0000313|Proteomes:UP000191056};
RN   [1] {ECO:0000313|EMBL:OPJ65871.1, ECO:0000313|Proteomes:UP000191056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23318 {ECO:0000313|EMBL:OPJ65871.1,
RC   ECO:0000313|Proteomes:UP000191056};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium chromiireducens DSM 23318.";
RL   Submitted (MAR-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ65871.1}.
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DR   EMBL; MZGT01000004; OPJ65871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4J0M5; -.
DR   STRING; 225345.CLCHR_04440; -.
DR   Proteomes; UP000191056; 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; 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:UP000191056};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   441 AA;  49207 MW;  9921FD6966BBFE18 CRC64;
     MKNLIYVGRD NNYMNNAQEL LDFINKGKTA FQSTYEIKDI LDKQGYTEIK EEDKWELKKG
     GKHYIIKNDS ALIAFEIGNG DIEKDGFRLI GAHTDSPGFR IKPNPEMKVE GHYVKLNTEV
     YGGPILSTWF DRPLSIAGRV TLKGENPFNP KVELLDVNKP ILIIPNLAIH MNRSVNEGYE
     YNKQKDTLPM LALVEDKLEK DNYLINLIAE TLKVDSSDIL DFDLFLYEYA EGMLIGLNDE
     FISCGRLDDL WMVFAGLKAL ISSNQIKATK VLVALDNEEI GSLTSQGANS SILENILERI
     TLGLEKDRED FKRALSNSIM ISADLAHAIH PNYTEKCDPT NKPMLGMGPV LKIAAGGSYS
     TDSYASAVFK GICEKAEVPC QVFVNRSDLR GGTTIGPITA SKLNIPVIDM GAPLLSMHSI
     RELATVKDNE YTIKAFTEFF N
//