LAP_PSEAB
ID LAP_PSEAB Reviewed; 536 AA.
AC Q02PA2;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase;
DE AltName: Full=PaAP;
DE Flags: Precursor;
GN Name=lap {ECO:0000305}; OrderedLocusNames=PA14_26020;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT THR-196.
RC STRAIN=UCBPP-PA14;
RX PubMed=24965220; DOI=10.1002/pmic.201400190;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Extracellular Ser/Thr/Tyr phosphorylated proteins of Pseudomonas
RT aeruginosa PA14 strain.";
RL Proteomics 14:2017-2030(2014).
CC -!- FUNCTION: A secreted aminopeptidase. Acts on free N-terminal amino
CC groups with a very strong preference for Leu in the first position.
CC {ECO:0000250|UniProtKB:Q9HZQ8}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000438; ABJ12177.1; -; Genomic_DNA.
DR RefSeq; WP_003101464.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02PA2; -.
DR SMR; Q02PA2; -.
DR MEROPS; M28.008; -.
DR iPTMnet; Q02PA2; -.
DR PRIDE; Q02PA2; -.
DR EnsemblBacteria; ABJ12177; ABJ12177; PA14_26020.
DR KEGG; pau:PA14_26020; -.
DR HOGENOM; CLU_024336_0_2_6; -.
DR OMA; YRVNNCV; -.
DR BioCyc; PAER208963:G1G74-2171-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03876; M28_SGAP_like; 1.
DR InterPro; IPR029514; Ape3.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR PANTHER; PTHR12147:SF17; PTHR12147:SF17; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Disulfide bond; Hydrolase; Metal-binding; Phosphoprotein;
KW Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..536
FT /note="Aminopeptidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431391"
FT DOMAIN 152..255
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 466
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24965220"
FT DISULFID 465..470
FT /evidence="ECO:0000250|UniProtKB:P80561"
SQ SEQUENCE 536 AA; 57511 MW; EE57BEFFC11C803A CRC64;
MSNKNNLRYA LGALALSVSA ASLAAPSEAQ QFTEFWTPGK PNPSICKSPL LVSTPLGLPR
CLQASNVVKR LQKLEDIASL NDGNRAAATP GYQASVDYVK QTLQKAGYKV SVQPFPFTAY
YPKGPGSLSA TVPQPVTYEW EKDFTYLSQT EAGDVTAKVV PVDLSLGAGN TSTSGCEAED
FANFPAGSIA LIQRGTCNFE QKAENAAAAG AAGVIIFNQG NTDDRKGLEN VTVGESYEGG
IPVIFATYDN GVAWSQTPDL QLHLVVDVVR KKTETYNVVA ETRRGNPNNV VMVGAHLDSV
FEGPGINDNG SGSAAQLEMA VLLAKALPVN KVRFAWWGAE EAGLVGSTHY VQNLAPEEKK
KIKAYLNFDM IGSPNFGNFI YDGDGSDFGL QGPPGSAAIE RLFEAYFRLR GQQSEGTEID
FRSDYAEFFN SGIAFGGLFT GAEGLKTEEQ AQKYGGTAGK AYDECYHSKC DGIANINQDA
LEIHSDAMAF VTSWLSLSTK VVDDEIAAAG QKAQSRSLQM QKSASQIERW GHDFIK
