AMPA1_SHEON
ID AMPA1_SHEON Reviewed; 500 AA.
AC Q8EI85;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable cytosol aminopeptidase 1;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase 1;
DE Short=LAP 1;
DE EC=3.4.11.10;
DE AltName: Full=Leucyl aminopeptidase 1;
GN Name=pepA1; Synonyms=pepA-1; OrderedLocusNames=SO_0959;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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 (By similarity).
CC {ECO:0000250}.
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;
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN54033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014299; AAN54033.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_716588.1; NC_004347.2.
DR AlphaFoldDB; Q8EI85; -.
DR SMR; Q8EI85; -.
DR STRING; 211586.SO_0959; -.
DR PaxDb; Q8EI85; -.
DR KEGG; son:SO_0959; -.
DR PATRIC; fig|211586.12.peg.920; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_6_0_6; -.
DR OMA; HGFKRVC; -.
DR OrthoDB; 356206at2; -.
DR PhylomeDB; Q8EI85; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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..500
FT /note="Probable cytosol aminopeptidase 1"
FT /id="PRO_0000165796"
FT ACT_SITE 275
FT /evidence="ECO:0000255"
FT ACT_SITE 350
FT /evidence="ECO:0000255"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 500 AA; 53027 MW; 070041251E1BB338 CRC64;
MALACLNSLN ANAEIFSFDT RNSLNSDTLV LFHSADSTTY SLDFLPQSTQ DQLNLAVADN
SFSGKRGEVL EILVPSEIDA KRVLLVGIGD AKTLTPGEIN ALGGNIAAKL ETVPQATVRV
LTQGLNNAPL FGSELAHGIE LRSYRYTQFK ASNRVEKNYQ IGVDDLSLNQ KHHKNLQAVE
AGVFLARDLT NAPAGNMYPE SFANEARKLK SLGVKVTVLE AKDIERLNLG ALAAVGKGSE
RPPKLVVAHW PGSKEAPIAL VGKGITFDSG GYNIKATGTS IARMKSDMAG AATVLGTVKA
MAIQKAPVNL VAIMPMAENM VSGHAMIPGD VITTAQGLTV EVLNTDAEGR LVLADGLWYA
RENYRPSVII DVATLTGSKV SALGTVYAGL FTDSEPLVQQ LTFAGQQVGE KVWRLPLDQA
YDDELKSTIA DLKNTGKEGS AGASAAAMFL KRFAGDQPWA HLDIAGHALT ATDTAVVPAG
ATGYGVRLLS TWLTQPKAQN
