LAP_PSEAE
ID LAP_PSEAE Reviewed; 536 AA.
AC Q9HZQ8;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase;
DE AltName: Full=PaAP {ECO:0000303|PubMed:11533066};
DE Contains:
DE RecName: Full=Aminopeptidase AP58 {ECO:0000303|PubMed:9642203};
DE Contains:
DE RecName: Full=Aminopeptidase AP56 {ECO:0000303|PubMed:11533066};
DE Contains:
DE RecName: Full=Aminopeptidase AP28 {ECO:0000303|PubMed:11533066};
DE Flags: Precursor;
GN Name=lap {ECO:0000305}; OrderedLocusNames=PA2939;
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 [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).
RN [2]
RP PROTEIN SEQUENCE OF 25-34.
RC STRAIN=PAO1 / PAO25;
RX PubMed=9642203; DOI=10.1128/jb.180.13.3467-3469.1998;
RA Braun P., de Groot A., Bitter W., Tommassen J.;
RT "Secretion of elastinolytic enzymes and their propeptides by Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 180:3467-3469(1998).
RN [3]
RP PROTEIN SEQUENCE OF 39-58 AND 273-291, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1, and FRD2;
RX PubMed=11533066; DOI=10.1074/jbc.m106950200;
RA Cahan R., Axelrad I., Safrin M., Ohman D.E., Kessler E.;
RT "A secreted aminopeptidase of Pseudomonas aeruginosa. Identification,
RT primary structure, and relationship to other aminopeptidases.";
RL J. Biol. Chem. 276:43645-43652(2001).
CC -!- FUNCTION: A secreted aminopeptidase. Acts on free N-terminal amino
CC groups with a very strong preference for Leu- followed by Met- and
CC Ala-, and no activity on Glu- or Gly- peptides (an exhaustive analysis
CC was not performed). Both the AP56 and AP28 forms have activity.
CC {ECO:0000269|PubMed:11533066}.
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 Evidence={ECO:0000269|PubMed:11533066};
CC -!- ACTIVITY REGULATION: Mature protein inhibited by dithiothreitol and
CC Zn(2+) chelators such as 1,10-phenanthroline, EDTA and EGTA. Not
CC inhibited by serine-protease inhibitors, N-ethylmaleimide or
CC phosphoramidon (which inhibits elastase).
CC {ECO:0000269|PubMed:11533066}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5, active between pH 7 and 9.5.
CC {ECO:0000269|PubMed:11533066};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11533066}.
CC -!- PTM: Processing of the 56 kDa pro-protein to mature protein requires
CC elastase (lasB); in vitro it only occurs at greater than 55 degrees
CC Celsius. {ECO:0000269|PubMed:11533066}.
CC -!- PTM: Several forms of the enzyme have been identified by molecular
CC weight, exactly which part of the sequence they correspond to is not
CC always clear. The AP58 form may be subject to proteolysis to give rise
CC to AP56. {ECO:0000305|PubMed:11533066, ECO:0000305|PubMed:9642203}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG06327.1; -; Genomic_DNA.
DR PIR; B83278; B83278.
DR RefSeq; NP_251629.1; NC_002516.2.
DR RefSeq; WP_003101464.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; Q9HZQ8; -.
DR SMR; Q9HZQ8; -.
DR STRING; 287.DR97_5001; -.
DR MEROPS; M28.003; -.
DR MEROPS; M28.008; -.
DR PaxDb; Q9HZQ8; -.
DR PRIDE; Q9HZQ8; -.
DR DNASU; 882792; -.
DR EnsemblBacteria; AAG06327; AAG06327; PA2939.
DR GeneID; 882792; -.
DR KEGG; pae:PA2939; -.
DR PATRIC; fig|208964.12.peg.3082; -.
DR PseudoCAP; PA2939; -.
DR HOGENOM; CLU_024336_0_2_6; -.
DR InParanoid; Q9HZQ8; -.
DR OMA; YRVNNCV; -.
DR PhylomeDB; Q9HZQ8; -.
DR BioCyc; PAER208964:G1FZ6-2989-MON; -.
DR BRENDA; 3.4.11.1; 5087.
DR Proteomes; UP000002438; 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:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:PseudoCAP.
DR GO; GO:0006508; P:proteolysis; IDA:PseudoCAP.
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; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:9642203"
FT CHAIN 25..536
FT /note="Aminopeptidase AP58"
FT /evidence="ECO:0000269|PubMed:9642203"
FT /id="PRO_0000431392"
FT CHAIN 39..536
FT /note="Aminopeptidase AP56"
FT /evidence="ECO:0000269|PubMed:11533066"
FT /id="PRO_0000431393"
FT CHAIN 273..536
FT /note="Aminopeptidase AP28"
FT /evidence="ECO:0000269|PubMed:11533066"
FT /id="PRO_0000431394"
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 DISULFID 465..470
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT VARIANT 46
FT /note="C -> A (in strain: FRD2)"
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
