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AMPA_SALAR
ID   AMPA_SALAR              Reviewed;         503 AA.
AC   A9MET9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=SARI_03166;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX23005.1; -; Genomic_DNA.
DR   RefSeq; WP_000397141.1; NC_010067.1.
DR   AlphaFoldDB; A9MET9; -.
DR   SMR; A9MET9; -.
DR   STRING; 41514.SARI_03166; -.
DR   MEROPS; M17.003; -.
DR   EnsemblBacteria; ABX23005; ABX23005; SARI_03166.
DR   KEGG; ses:SARI_03166; -.
DR   HOGENOM; CLU_013734_2_2_6; -.
DR   OMA; MKNTGPR; -.
DR   OrthoDB; 356206at2; -.
DR   Proteomes; UP000002084; 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..503
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_1000077282"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         293
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         354
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   BINDING         354
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   503 AA;  54920 MW;  72B3E7F601311A9D CRC64;
     MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL
     LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR
     NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAIQHGLAI
     AAGIKAAKDL GNMPPNICNA AYLASQARQL ADSYSKKVIT RVIGEQQMRE LGMNAYLAVG
     HGSQNESLMS VIEYKGNPSE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV
     YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC
     DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMSNHN PLAHELLGAS EQAGDRAWRL
     PLGDEYQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG
     ATGRPVALLS QFLLNRAGFN GEE
 
 
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