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Database: UniProt
Entry: A0A1J0GL53_9CLOT
LinkDB: A0A1J0GL53_9CLOT
Original site: A0A1J0GL53_9CLOT 
ID   A0A1J0GL53_9CLOT        Unreviewed;       433 AA.
AC   A0A1J0GL53;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   ORFNames=A7L45_19745 {ECO:0000313|EMBL:APC42130.1};
OS   Clostridium estertheticum subsp. estertheticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1552 {ECO:0000313|EMBL:APC42130.1, ECO:0000313|Proteomes:UP000182569};
RN   [1] {ECO:0000313|Proteomes:UP000182569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8809 {ECO:0000313|Proteomes:UP000182569};
RX   PubMed=27891116;
RA   Yu Z., Gunn L., Brennan E., Reid R., Wall P.G., Gaora O.P., Hurley D.,
RA   Bolton D., Fanning S.;
RT   "Complete Genome Sequence of Clostridium estertheticum DSM 8809, a Microbe
RT   Identified in Spoiled Vacuum Packed Beef.";
RL   Front. Microbiol. 7:1764-1764(2016).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467,
CC       ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP015756; APC42130.1; -; Genomic_DNA.
DR   RefSeq; WP_071614421.1; NZ_CP015756.1.
DR   AlphaFoldDB; A0A1J0GL53; -.
DR   STRING; 1552.A7L45_19745; -.
DR   KEGG; ceu:A7L45_19745; -.
DR   OrthoDB; 9764268at2; -.
DR   Proteomes; UP000182569; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
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, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW   Rule:MF_00467};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182569};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}.
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT   BINDING         409
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
SQ   SEQUENCE   433 AA;  48076 MW;  0790207312BE358E CRC64;
     MSKKLEFAQN LIDYIYDSPT AYHAVAKAKG DLCKAGFVEI KEEDKWELKK GGKYFVTKND
     SALTAFVVGK GEIEESGFKI IGAHTDSPSF RIKPSPEMVV DNVYVRLNTE VYGGPILNTW
     MDRPLAIAGR VTLRSEDILH PETRLVNIKR PIMIIPNLAI HMNRNVNAGI ELNKQKDLLP
     LLSMVNENLE KNNYLISAIA KELAVDLKEI IDFDLFLYEY EKGSIIGLNN EFISSSRLDD
     LAMVHAGISA ISRGSSVQAT NVIVCFDNEE VGSSTKQGAD SNMLVDILER ITISLHKNRE
     EFFRAISKSF IISADNAHAV HPNSPEKNDP TNKPYINKGP VIKISASQSY TTDSNSDAVY
     ELICEKAGVP IQKFVNRSDA RGGSTIGPIS STHLNIRSVD MGSPTLAMHS IRELGGVLDH
     FYVTKSFEEF YKI
//
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