ID   APEB_CLOAB              Reviewed;         433 AA.
AC   Q97LF4;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Probable M18 family aminopeptidase 2;
DE            EC=3.4.11.-;
GN   Name=apeB; OrderedLocusNames=CA_C0607;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR   EMBL; AE001437; AAK78585.1; -; Genomic_DNA.
DR   PIR; F96974; F96974.
DR   RefSeq; NP_347245.1; NC_003030.1.
DR   RefSeq; WP_010963927.1; NC_003030.1.
DR   AlphaFoldDB; Q97LF4; -.
DR   SMR; Q97LF4; -.
DR   STRING; 272562.CA_C0607; -.
DR   EnsemblBacteria; AAK78585; AAK78585; CA_C0607.
DR   GeneID; 44997118; -.
DR   KEGG; cac:CA_C0607; -.
DR   PATRIC; fig|272562.8.peg.810; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_9; -.
DR   OMA; KSGCHAI; -.
DR   OrthoDB; 304020at2; -.
DR   Proteomes; UP000000814; 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_0000173461"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         409
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   433 AA;  48393 MW;  1D2DA40A9FD78A34 CRC64;
     MKNELEFAKK LIDFIYDSPS PFHSVDNIKN TLIENGFAEI KEENKWELNK NGKYFVKRND
     SALIAFTVGS GFVAKKGFKI IGGHTDSPTF RIKPNPEMVS ENSYIKLNTE VYGGPILSTW
     FDRPLSIAGR VTVRGKSALF PETKLLNIKR PILVIPNLAI HMNRDVNSGF KINPQVDTLP
     IIGIINDKFE KENYLMKIIA SELGEDIENI IDFDLFLYEY DKGCIMGINN EFISSSRLDD
     MEMVHAGLNA LVNAKCSEAT NVLACFDNEE IGSATKQGAD SQFLSDILER IVLSFGGDRE
     DFFRALHNSF MISSDSAHAV HPNKGEKADP ITRPHINEGP VIKISAAQKY TSDSNSIAVY
     EEVCRLSGVP YQKFVNRSDE RGGSTIGPIT ATHTAIRTVD IGTPLLAMHS IRELCGTLDH
     MYVEKSFEEF YNL