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AMPA_HAMD5
ID   AMPA_HAMD5              Reviewed;         501 AA.
AC   C4K346;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Probable cytosol aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.1 {ECO:0000255|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE            Short=LAP {ECO:0000255|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.10 {ECO:0000255|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
GN   Name=pepA {ECO:0000255|HAMAP-Rule:MF_00181}; OrderedLocusNames=HDEF_0221;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
CC   -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC       intracellular proteins. Catalyzes the removal of unsubstituted N-
CC       terminal amino acids from various peptides. {ECO:0000255|HAMAP-
CC       Rule:MF_00181}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC         is preferably Leu, but may be other amino acids including Pro
CC         although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC         methyl esters are also readily hydrolyzed, but rates on arylamides
CC         are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00181};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, preferentially leucine,
CC         but not glutamic or aspartic acids.; EC=3.4.11.10;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00181};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00181}.
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DR   EMBL; CP001277; ACQ66989.1; -; Genomic_DNA.
DR   RefSeq; WP_012737954.1; NC_012751.1.
DR   AlphaFoldDB; C4K346; -.
DR   SMR; C4K346; -.
DR   STRING; 572265.HDEF_0221; -.
DR   MEROPS; M17.003; -.
DR   EnsemblBacteria; ACQ66989; ACQ66989; HDEF_0221.
DR   GeneID; 66260147; -.
DR   KEGG; hde:HDEF_0221; -.
DR   eggNOG; COG0260; Bacteria.
DR   HOGENOM; CLU_013734_2_2_6; -.
DR   OMA; MKNTGPR; -.
DR   Proteomes; UP000002334; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00433; Peptidase_M17; 1.
DR   Gene3D; 3.40.220.10; -; 1.
DR   HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   PANTHER; PTHR11963; PTHR11963; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease;
KW   Reference proteome.
FT   CHAIN           1..501
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_1000203831"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         267
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         272
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         272
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         290
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         349
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         351
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         351
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   501 AA;  54386 MW;  9309E6D3AA48CE91 CRC64;
     MEFKVNSECS EKQSSDCIVI GIFESGEFSP SAEKVNKISH GYLKGLPQNA DLQGKAEQAL
     LLHHVPHVAA ERVLLIGCGK EEELDERRYK KLIKKMVNTL KETGAKNVFC YLPELKVKGK
     DIDWKIRSAI EVIQDALYCF DHYKSTKTLH ALNQITFIVT ATQTKAAQTA IQEGIALAVG
     INEAKNLANT PPNICNPAYL NASARKWAEK FKNVRVSVVN EDEMKKLGMN AYLAVGQGSK
     NESLMSIIEY KSGKIPAGTK PIVLVGKGMT FDSGGISIKP SQNMDEMKYD MCGAATVFGV
     MNVVAELNLP LYVIGVLAGA ENMPGGNAYR PGDILTTLSG QTVEVLNTDA EGRLVLCDAL
     TYVERFDPEL VIDIATLTGA CVVALGHHMS GLMSNHAPLA EDLLHASEQS GDLAWRLPLG
     EEYQEQLDSN FADMANIGGR TAGAITAGCF LSRFTHQYHW AHLDIAGTAW RTGKEKGATG
     RPVALLSQFL LNKALAQKQG A
 
 
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