ID   APEB_CLONN              Reviewed;         433 AA.
AC   A0PYH7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000255|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000255|HAMAP-Rule:MF_00467}; OrderedLocusNames=NT01CX_1346;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00467};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00467}.
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DR   EMBL; CP000382; ABK61088.1; -; Genomic_DNA.
DR   RefSeq; WP_011721437.1; NC_008593.1.
DR   AlphaFoldDB; A0PYH7; -.
DR   SMR; A0PYH7; -.
DR   STRING; 386415.NT01CX_1346; -.
DR   EnsemblBacteria; ABK61088; ABK61088; NT01CX_1346.
DR   KEGG; cno:NT01CX_1346; -.
DR   PATRIC; fig|386415.7.peg.454; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_9; -.
DR   OMA; KSGCHAI; -.
DR   OrthoDB; 304020at2; -.
DR   Proteomes; UP000008220; 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   Gene3D; 2.30.250.10; -; 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; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..433
FT                   /note="Probable M18 family aminopeptidase 2"
FT                   /id="PRO_1000013697"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT   BINDING         409
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
SQ   SEQUENCE   433 AA;  48293 MW;  E65BE5E48B548214 CRC64;
     MKNKIKFANE LLDFIYKSPT AFHAVDTIKK VLNKEGFSEL KECEKWNIEK GKKYYMTKND
     SAIVAFVVGN GEVHEDGFKI IGAHTDSPTF RIKPNPEMTS EQSYIKLNTE VYGGPILNTW
     IDRPLAVAGR VTLKGENILF PETKLVNINK PIMIIPNLAI HMNRNINQGI ELNRQVDTLP
     ILGLINDKFE KNDYLLKAIA KELDVDYKEI IDFDLFLYEY EKGSIIGIEN EFVSSGRLDD
     LEAVHAALEG LTQSNVSKAT NVLVCFDNEE VGSSTKQGAD SNMLANVLER IVISLNGDRE
     DFFRALSKSF IISSDSAHAV HPNKGEKCDP TNRPKLNKGP AIKIAASQSY TSDSNSSSVF
     KALCSKADVP VQEFVNRSDE RGGSTIGPIS STHLNIRSVD IGTPLLAMHS IRELCGVDDH
     YYGMKVFKEF YNL