AMPA_PSEPU
ID AMPA_PSEPU Reviewed; 497 AA.
AC O86436;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
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;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC
RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90;
RA Sonke T., Kaptein B., Boesten W.H.J., Broxterman Q.B., Kamphuis J.,
RA Formaggio F., Toniolo C., Rutjes F.P.J.T., Schoemaker H.E.;
RT "New developments in the enzymatic preparation and use of enantiopure
RT alpha-hydrogen and alpha,alpha-disubstituted alpha-amino acids.";
RL Submitted (AUG-1998) 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 (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; AJ010261; CAA09054.1; -; Genomic_DNA.
DR RefSeq; WP_016501309.1; NZ_WOWR01000017.1.
DR PDB; 3H8E; X-ray; 2.75 A; A/B=1-497.
DR PDB; 3H8F; X-ray; 2.20 A; A/B/C/D/E/F=1-497.
DR PDB; 3H8G; X-ray; 1.50 A; A/B/C/D/E/F=1-497.
DR PDBsum; 3H8E; -.
DR PDBsum; 3H8F; -.
DR PDBsum; 3H8G; -.
DR AlphaFoldDB; O86436; -.
DR SMR; O86436; -.
DR STRING; 1240350.AMZE01000025_gene1699; -.
DR MEROPS; M17.003; -.
DR GeneID; 45525812; -.
DR eggNOG; COG0260; Bacteria.
DR BRENDA; 3.4.11.10; 5092.
DR EvolutionaryTrace; O86436; -.
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 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Protease.
FT CHAIN 1..497
FT /note="Cytosol aminopeptidase"
FT /id="PRO_0000165783"
FT ACT_SITE 279
FT /evidence="ECO:0000255"
FT ACT_SITE 353
FT /evidence="ECO:0000255"
FT BINDING 267
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:3H8G"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3H8G"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 166..191
FT /evidence="ECO:0007829|PDB:3H8G"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 292..307
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 310..322
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 352..363
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 379..385
FT /evidence="ECO:0007829|PDB:3H8G"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 397..410
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 443..452
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:3H8G"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:3H8G"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:3H8G"
FT HELIX 484..495
FT /evidence="ECO:0007829|PDB:3H8G"
SQ SEQUENCE 497 AA; 52469 MW; 69851EB412B7F81A CRC64;
MELVVKSVAA ASVKTATLVI PVGENRKLGA VAKAVDLASE GAISAVLKRG DLAGKPGQTL
LLQNLQGLKA ERVLLVGSGK DEALGDRTWR KLVASVAGVL KGLNGADAVL ALDDVAVNNR
DAHYGKYRLL AETLLDGEYV FDRFKSQKVE PRALKKVTLL ADKAGQAEVE RAVKHASAIA
TGMAFTRDLG NLPPNLCHPS FLAEQAKELG KAHKALKVEV LDEKKIKDLG MGAFYAVGQG
SDQPPRLIVL NYQGGKKADK PFVLVGKGIT FDTGGISLKP GAGMDEMKYD MCGAASVFGT
LRAVLELQLP VNLVCLLACA ENMPSGGATR PGDIVTTMSG QTVEILNTDA EGRLVLCDTL
TYAERFKPQA VIDIATLTGA CIVALGSHTT GLMGNNDDLV GQLLDAGKRA DDRAWQLPLF
DEYQEQLDSP FADMGNIGGP KAGTITAGCF LSRFAKAYNW AHMDIAGTAW ISGGKDKGAT
GRPVPLLTQY LLDRAGA
