IMPA_PSEAE
ID IMPA_PSEAE Reviewed; 923 AA.
AC Q9I5W4;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Immunomodulating metalloprotease {ECO:0000303|PubMed:22309196};
DE EC=3.4.24.- {ECO:0000269|PubMed:22309196};
DE AltName: Full=IMPa {ECO:0000303|PubMed:22309196};
DE Flags: Precursor;
GN Name=impA {ECO:0000303|PubMed:22309196};
GN OrderedLocusNames=PA0572 {ECO:0000312|EMBL:AAG03961.1};
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 FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, ACTIVITY REGULATION, AND COFACTOR.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=22309196; DOI=10.1111/j.1462-5822.2012.01765.x;
RA Bardoel B.W., Hartsink D., Vughs M.M., de Haas C.J., van Strijp J.A.,
RA van Kessel K.P.;
RT "Identification of an immunomodulating metalloprotease of Pseudomonas
RT aeruginosa (IMPa).";
RL Cell. Microbiol. 14:902-913(2012).
CC -!- FUNCTION: Protease that degrades several proteins of the host immune
CC system. Cleaves P-selectin glycoprotein ligand-1 (PSGL-1), leading to
CC its functional inhibition; PSGL-1 is a leukocyte cell-surface receptor
CC essential for leukocyte recruitment to the site of infection. Next to
CC PSGL-1, targets host CD43 and CD44 that are also involved in leukocyte
CC homing. Thus, prevents neutrophil extravasation and thereby protects
CC P.aeruginosa from neutrophil attack. Is also able to inhibit the decay
CC accelerating factor (CD55), but not the cell-surface receptors CD46 and
CC CD31. {ECO:0000269|PubMed:22309196}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Proteolytic activity is blocked in the presence of
CC EDTA. {ECO:0000269|PubMed:22309196}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22309196}.
CC -!- SIMILARITY: Belongs to the peptidase M88 family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03961.1; -; Genomic_DNA.
DR PIR; E83574; E83574.
DR RefSeq; NP_249263.1; NC_002516.2.
DR RefSeq; WP_003142775.1; NZ_QZGE01000010.1.
DR PDB; 5KDV; X-ray; 1.93 A; A=42-923.
DR PDB; 5KDW; X-ray; 1.85 A; A/B=42-923.
DR PDB; 5KDX; X-ray; 2.40 A; A/B=42-923.
DR PDB; 7JTV; X-ray; 2.45 A; A/B=42-923.
DR PDBsum; 5KDV; -.
DR PDBsum; 5KDW; -.
DR PDBsum; 5KDX; -.
DR PDBsum; 7JTV; -.
DR AlphaFoldDB; Q9I5W4; -.
DR SMR; Q9I5W4; -.
DR STRING; 287.DR97_3540; -.
DR MEROPS; M88.001; -.
DR PaxDb; Q9I5W4; -.
DR PRIDE; Q9I5W4; -.
DR DNASU; 878237; -.
DR EnsemblBacteria; AAG03961; AAG03961; PA0572.
DR GeneID; 878237; -.
DR KEGG; pae:PA0572; -.
DR PATRIC; fig|208964.12.peg.604; -.
DR PseudoCAP; PA0572; -.
DR HOGENOM; CLU_004117_0_0_6; -.
DR InParanoid; Q9I5W4; -.
DR OMA; NPYDAYW; -.
DR BioCyc; PAER208964:G1FZ6-578-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR GO; GO:1903237; P:negative regulation of leukocyte tethering or rolling; IDA:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IDA:UniProtKB.
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; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.30; -; 1.
DR InterPro; IPR041549; IMPa_helical.
DR InterPro; IPR040711; IMPa_N_2.
DR InterPro; IPR042279; Pep_M60_3.
DR InterPro; IPR031161; Peptidase_M60_dom.
DR Pfam; PF18642; IMPa_helical; 1.
DR Pfam; PF18650; IMPa_N_2; 1.
DR Pfam; PF13402; Peptidase_M60; 1.
DR SMART; SM01276; M60-like; 1.
DR PROSITE; PS51723; PEPTIDASE_M60; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..923
FT /note="Immunomodulating metalloprotease"
FT /id="PRO_5004328522"
FT DOMAIN 450..794
FT /note="Peptidase M60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01060"
FT ACT_SITE 697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 696
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 700
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 63..89
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 147..151
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 274..280
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:7JTV"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 339..358
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 370..385
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 392..395
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 396..406
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 448..459
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:7JTV"
FT STRAND 524..532
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 538..545
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:5KDX"
FT HELIX 561..573
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 586..591
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 592..603
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 607..616
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 619..625
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 637..645
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 653..656
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 662..668
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 678..685
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 692..702
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 711..714
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 715..720
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 721..733
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 745..755
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 761..769
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 775..778
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 779..796
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 800..804
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 805..819
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 822..825
FT /evidence="ECO:0007829|PDB:5KDW"
FT TURN 826..830
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 848..861
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 866..871
FT /evidence="ECO:0007829|PDB:5KDW"
FT HELIX 878..886
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 895..898
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 900..903
FT /evidence="ECO:0007829|PDB:5KDV"
FT HELIX 905..907
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 909..912
FT /evidence="ECO:0007829|PDB:5KDW"
FT STRAND 914..916
FT /evidence="ECO:0007829|PDB:5KDV"
SQ SEQUENCE 923 AA; 100155 MW; D15BA201FE964769 CRC64;
MSLSTTAFPS LQGENMSRSP IPRHRALLAG FCLAGALSAQ AATQEEILDA ALVSGDSSQL
TDSHLVALRL QQQVERIRQT RTQLLDGLYQ NLSQAYDPGA ASMWVLPANP DNTLPFLIGD
KGRVLASLSL EAGGRGLAYG TNVLTQLSGT NAAHAPLLKR AVQWLVNGDP GAATAKDFKV
SVVGVDKTAA LNGLKSAGLQ PADAACNALT DASCASTSKL LVLGNGASAA SLSATVRARL
QAGLPILFVH TNGWNQSSTG QQILAGLGLQ EGPYGGNYWD KDRVPSSRTR TRSVELGGAY
GQDPALVQQI VDGSWRTDYD WSKCTSYVGR TTCDDVPGLS DFSKRVDVLK GALDAYNQKA
QNLFALPGTT SLRLWLLWAD AVRQNIRYPM DKAADTARFQ ETFVADAIVG YVREAGAAQK
ELGSYAGQRQ QSMPVSGSEE TLTLTLPSAQ GFTAIGRMAA PGKRLSIRIE DAGQASLAVG
LNTQRIGSTR LWNTRQYDRP RFLKSPDIKL QANQSVALVS PYGGLLQLVY SGATPGQTVT
VKVTGAASQP FLDIQPGEDS SQAIADFIQA LDADKADWLE IRSGSVEVHA KVEKVRGSID
KDYGGDVQRF IRELNEVFID DAYTLAGFAI PNQAKTPAIQ QECAARGWDC DSETLHKLPG
TQHINVDQYA QCGGGCSGNP YDQTWGLNPR GWGESHELGH NLQVNRLKVY GGRSGEISNQ
IFPLHKDWRV LREFGQNLDD TRVNYRNAYN LIVAGRAEAD PLAGVYKRLW EDPGTYALNG
ERMAFYTQWV HYWADLKNDP LQGWDIWTLL YLHQRQVDKS DWDANKAALG YGTYAQRPGN
SGDASSTDGN DNLLLGLSWL TQRDQRPTFA LWGIRTSAAA QAQVAAYGFA EQPAFFYANN
RTNEYSTVKL LDMSQGSPAW PFP
