ID   L1QND0_9CLOT            Unreviewed;       206 AA.
AC   L1QND0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF0216_00436 {ECO:0000313|EMBL:EKY29077.1};
OS   Clostridium celatum DSM 1785.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=545697 {ECO:0000313|EMBL:EKY29077.1, ECO:0000313|Proteomes:UP000010420};
RN   [1] {ECO:0000313|EMBL:EKY29077.1, ECO:0000313|Proteomes:UP000010420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1785 {ECO:0000313|EMBL:EKY29077.1,
RC   ECO:0000313|Proteomes:UP000010420};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {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:EKY29077.1}.
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DR   EMBL; AMEZ01000013; EKY29077.1; -; Genomic_DNA.
DR   AlphaFoldDB; L1QND0; -.
DR   STRING; 545697.HMPREF0216_00436; -.
DR   PATRIC; fig|545697.3.peg.429; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_1_0_9; -.
DR   Proteomes; UP000010420; 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   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
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; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EKY29077.1}; Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010420};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   206 AA;  21983 MW;  BBFD1311D555FB20 CRC64;
     MNEELISSGR FDDLWMVYAG IKALVDSREN AATKVMICVD NEEIGSLTAE GANSTLLNNI
     LERIALGLGK DREGYYRALA NSIMISADLA HAVHPNLGDK HDPTNRPVLE GGPVLKIAAS
     GSYSTDSFNG AVFAGVCEAA GVPFQKFVNR SDVRGGTTIG PVTAANLTIP VIDMGAPVLG
     MHSIRELASV KDNYYTVKAF TEFFSL
//