AMPA_PSEAE
ID AMPA_PSEAE Reviewed; 495 AA.
AC O68822;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase;
DE Short=LAP;
DE EC=3.4.11.10;
DE AltName: Full=Leucyl aminopeptidase;
GN Name=pepA; Synonyms=phpA; OrderedLocusNames=PA3831;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FRD1;
RX PubMed=9864319; DOI=10.1128/jb.181.1.107-116.1999;
RA Woolwine S.C., Wozniak D.J.;
RT "Identification of an Escherichia coli pepA homolog and its involvement in
RT suppression of the algB phenotype in mucoid Pseudomonas aeruginosa.";
RL J. Bacteriol. 181:107-116(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
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DR EMBL; AF054622; AAD04821.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07218.1; -; Genomic_DNA.
DR PIR; D83167; D83167.
DR RefSeq; NP_252520.1; NC_002516.2.
DR RefSeq; WP_003092867.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; O68822; -.
DR SMR; O68822; -.
DR STRING; 287.DR97_4035; -.
DR MEROPS; M17.003; -.
DR PaxDb; O68822; -.
DR PRIDE; O68822; -.
DR EnsemblBacteria; AAG07218; AAG07218; PA3831.
DR GeneID; 879865; -.
DR KEGG; pae:PA3831; -.
DR PATRIC; fig|208964.12.peg.4011; -.
DR PseudoCAP; PA3831; -.
DR HOGENOM; CLU_013734_2_2_6; -.
DR InParanoid; O68822; -.
DR OMA; MKNTGPR; -.
DR PhylomeDB; O68822; -.
DR BioCyc; PAER208964:G1FZ6-3903-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; 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 GO; GO:0016070; P:RNA metabolic process; IMP:PseudoCAP.
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..495
FT /note="Cytosol aminopeptidase"
FT /id="PRO_0000165782"
FT ACT_SITE 278
FT /evidence="ECO:0000255"
FT ACT_SITE 352
FT /evidence="ECO:0000255"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
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 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 495 AA; 52332 MW; E08C7928E7A0FCDC CRC64;
MEFLVKSVRP ETLKTATLVL AVGEGRKLGA SAKAVDDATG GAISAVLKRG DLAGKVGQTL
LLQSLPNLKA ERVLLVGAGK ERELGDRQYR KLASAVLSTL KGLAGADAAL ALGDLAVKGR
DAHAKARLLV ETLADGLYVF DRYKSQKAEP LKLKKLTLLA DKADSAAVEQ GSKEAQAIAN
GMALTRDLGN LPPNVCHPTF LGEQAKGLAK EFKGLKVEVL DEKKLRELGM GSFLAVAQGS
DQPPRLIVLQ YNGAKKDQAP HVLVGKGITF DTGGISLKPG LGMDEMKFDM CGAASVFGTF
RAVLELQLPI NLVGLLACAE NMPSGGATRP GDIVTTMSGQ TVEILNTDAE GRLVLCDALT
YAERFKPQSV IDIATLTGAC IVALGSNTSG LMGNNEALVR QLLKAGEFAD DRAWQLPLFD
EYQEQLDSPF ADIANIGGPK AGTITAGCFL SRFAKKYHWA HLDIAGTAWI SGGKDKGATG
RPVPLLTQYL LERAK
