ID   AMP2_GEOSE              Reviewed;         413 AA.
AC   P24828;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Aminopeptidase 2;
DE            EC=3.4.11.- {ECO:0000269|PubMed:938681};
DE   AltName: Full=Aminopeptidase II;
DE            Short=AP-II;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX   PubMed=9362117; DOI=10.1271/bbb.61.1710;
RA   Motoshima H., Minagawa E., Tsukasaki F., Kaminogawa S.;
RT   "Cloning of genes of the aminopeptidase T family from Thermus thermophilus
RT   HB8 and Bacillus stearothermophilus NCIB8924: apparent similarity to the
RT   leucyl aminopeptidase family.";
RL   Biosci. Biotechnol. Biochem. 61:1710-1717(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX   PubMed=938681;
RA   Stoll E., Weder H.-G., Zuber H.;
RT   "Aminopeptidase II from Bacillus stearothermophilus.";
RL   Biochim. Biophys. Acta 438:213-220(1976).
CC   -!- FUNCTION: Broad specificity metal-dependent exopeptidase, releasing all
CC       N-terminal amino acids. {ECO:0000269|PubMed:938681}.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:938681};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P42778};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P42778};
CC       Note=Binds 2 divalent metal cations per subunit (PubMed:938681). Can
CC       use cobalt, zinc, and possibly also magnesium ions.
CC       {ECO:0000250|UniProtKB:P42778, ECO:0000269|PubMed:938681};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Highly thermostable. {ECO:0000269|PubMed:938681};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:938681}.
CC   -!- SIMILARITY: Belongs to the peptidase M29 family. {ECO:0000305}.
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DR   EMBL; D13385; BAA02653.1; -; Genomic_DNA.
DR   PIR; JC5863; JC5863.
DR   AlphaFoldDB; P24828; -.
DR   SMR; P24828; -.
DR   MEROPS; M29.002; -.
DR   BRENDA; 3.4.11.10; 623.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1830.10; -; 1.
DR   InterPro; IPR035097; M29_N-terminal.
DR   InterPro; IPR000787; Peptidase_M29.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   PRINTS; PR00919; THERMOPTASE.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cobalt; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..413
FT                   /note="Aminopeptidase 2"
FT                   /id="PRO_0000079173"
FT   BINDING         250
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         316
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         316
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         340
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         340
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         345
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         378
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         380
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
SQ   SEQUENCE   413 AA;  46210 MW;  624883F1C0D1FF87 CRC64;
     MNRWEKELDK YAELAVKVGV NIQPGQTLFV NAPLEAAPLV RKIAKTAYET GAKHVYFEWN
     DEALTYIKFH HAPEEAFSEY PMLRARAMEE LAEQGAAFLS IHAPNPDLLK DVDPKRIATA
     NKTAAQALAN YRSAIMADRN CWSLISVPTP AWAQKVFGDL RDEEAIDKLW EAIFRITRID
     QDDPIAAWRE HNDRLARIVD YLNNKQYKQL VYEAPGPIFT VELVDGHVWH GGAATSQSGV
     RFNPNIPTEE VFTMPHKDGV NGTVRNTKPL NYNGNVIDGF TLTFKDGQVV DFSAEQGYET
     LKHLLDTDDG ARRLGEVALV PHQSPVSLSN LIFYNTLFDE NAACHLALGK AYPTNIENGA
     SLSKEELDRR GVNDSLVHVD FMIGSADLNI DGVTKDGKRE PIFRSGNWAF ELA