APRA_PSEAE
ID APRA_PSEAE Reviewed; 479 AA.
AC Q03023;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Serralysin;
DE EC=3.4.24.40;
DE AltName: Full=Alkaline metalloproteinase;
DE Short=AP;
DE Flags: Precursor;
GN Name=aprA; OrderedLocusNames=PA1249;
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=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1427098; DOI=10.1016/0378-1119(92)90160-q;
RA Duong F., Lazdunski A., Cami B., Murgier M.;
RT "Sequence of a cluster of genes controlling synthesis and secretion of
RT alkaline protease in Pseudomonas aeruginosa: relationships to other
RT secretory pathways.";
RL Gene 121:47-54(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 13130 / JCM 20134;
RX PubMed=2123832; DOI=10.1128/iai.58.12.4083-4088.1990;
RA Okuda K., Morihara K., Atsumi Y., Takeuchi H., Kawamoto S., Kawasaki H.,
RA Suzuki K., Fukushima J.;
RT "Complete nucleotide sequence of the structural gene for alkaline
RT proteinase from Pseudomonas aeruginosa IFO 3455.";
RL Infect. Immun. 58:4083-4088(1990).
RN [3]
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 [4]
RP CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=4199986; DOI=10.1016/0005-2744(73)90040-5;
RA Morihara K., Tsuzuki H., Oka T.;
RT "On the specificity of Pseudomonas aeruginosa alkaline proteinase with
RT synthetic peptides.";
RL Biochim. Biophys. Acta 309:414-429(1973).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ZINC.
RX PubMed=8253063; DOI=10.1002/j.1460-2075.1993.tb06009.x;
RA Baumann U., Wu S., Flaherty K.M., McKay D.B.;
RT "Three-dimensional structure of the alkaline protease of Pseudomonas
RT aeruginosa: a two-domain protein with a calcium binding parallel beta roll
RT motif.";
RL EMBO J. 12:3357-3364(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 10-479 IN COMPLEX WITH CALCIUM AND
RP ZINC.
RC STRAIN=ATCC 21636 / NBRC 3080;
RX PubMed=8690704; DOI=10.1093/oxfordjournals.jbchem.a124932;
RA Miyatake H., Hata Y., Fujii T., Hamada K., Morihara K., Katsube Y.;
RT "Crystal structure of the unliganded alkaline protease from Pseudomonas
RT aeruginosa IFO3080 and its conformational changes on ligand binding.";
RL J. Biochem. 118:474-479(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 10-479 IN COMPLEX WITH CALCIUM;
RP ZINC AND ITS COGNATE INHIBITOR INH.
RX PubMed=11445573; DOI=10.1074/jbc.m104020200;
RA Hege T., Feltzer R.E., Gray R.D., Baumann U.;
RT "Crystal structure of a complex between Pseudomonas aeruginosa alkaline
RT protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative
RT bond.";
RL J. Biol. Chem. 276:35087-35092(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC P1'.; EC=3.4.24.40; Evidence={ECO:0000269|PubMed:4199986};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 8 Ca(2+) ions per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase M10B family. {ECO:0000305}.
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DR EMBL; X64558; CAA45858.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04638.1; -; Genomic_DNA.
DR PIR; A41463; A41463.
DR PIR; S26699; S26699.
DR RefSeq; NP_249940.1; NC_002516.2.
DR RefSeq; WP_003082542.1; NZ_QZGE01000005.1.
DR PDB; 1AKL; X-ray; 2.00 A; A=10-479.
DR PDB; 1JIW; X-ray; 1.74 A; P=10-479.
DR PDB; 1KAP; X-ray; 1.64 A; P=1-479.
DR PDB; 3VI1; X-ray; 2.00 A; A/B=10-479.
DR PDBsum; 1AKL; -.
DR PDBsum; 1JIW; -.
DR PDBsum; 1KAP; -.
DR PDBsum; 3VI1; -.
DR AlphaFoldDB; Q03023; -.
DR SMR; Q03023; -.
DR MINT; Q03023; -.
DR STRING; 287.DR97_688; -.
DR MEROPS; M10.056; -.
DR PaxDb; Q03023; -.
DR PRIDE; Q03023; -.
DR EnsemblBacteria; AAG04638; AAG04638; PA1249.
DR GeneID; 881248; -.
DR KEGG; pae:PA1249; -.
DR PATRIC; fig|208964.12.peg.1297; -.
DR PseudoCAP; PA1249; -.
DR HOGENOM; CLU_025059_1_1_6; -.
DR InParanoid; Q03023; -.
DR OMA; WYLINSS; -.
DR PhylomeDB; Q03023; -.
DR BioCyc; PAER208964:G1FZ6-1274-MON; -.
DR BRENDA; 3.4.24.40; 5087.
DR EvolutionaryTrace; Q03023; -.
DR PHI-base; PHI:4152; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IDA:PseudoCAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IDA:PseudoCAP.
DR GO; GO:0001869; P:negative regulation of complement activation, lectin pathway; IDA:PseudoCAP.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IDA:PseudoCAP.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04277; ZnMc_serralysin_like; 1.
DR Gene3D; 2.150.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR016294; Pept_M10B.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR034033; Serralysin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF00353; HemolysinCabind; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR PIRSF; PIRSF001205; Peptidase_M10B; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; SSF51120; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Zinc; Zymogen.
FT PROPEP 1..9
FT /id="PRO_0000028681"
FT CHAIN 10..479
FT /note="Serralysin"
FT /id="PRO_0000028682"
FT REPEAT 341..354
FT /note="Hemolysin-type calcium-binding 1"
FT /evidence="ECO:0000305"
FT REPEAT 355..367
FT /note="Hemolysin-type calcium-binding 2"
FT /evidence="ECO:0000305"
FT REPEAT 368..385
FT /note="Hemolysin-type calcium-binding 3"
FT /evidence="ECO:0000305"
FT ACT_SITE 186
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT VARIANT 127
FT /note="D -> H (in strain: IFO 3455)"
FT VARIANT 176
FT /note="G -> A (in strain: IFO 3455)"
FT VARIANT 195..197
FT /note="HPG -> T (in strain: IFO 3455)"
FT VARIANT 350
FT /note="I -> Y (in strain: IFO 3455)"
FT VARIANT 388..389
FT /note="GD -> A (in strain: IFO 3455)"
FT VARIANT 391..392
FT /note="AE -> SP (in strain: IFO 3455)"
FT VARIANT 394..396
FT /note="SAA -> PPR (in strain: IFO 3455)"
FT VARIANT 435..439
FT /note="KAGQA -> NAQG (in strain: IFO 3455)"
FT VARIANT 454
FT /note="I -> V (in strain: IFO 3455)"
FT VARIANT 460
FT /note="A -> R (in strain: IFO 3455)"
FT VARIANT 479
FT /note="V -> L (in strain: IFO 3455)"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1KAP"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:1KAP"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 116..127
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1KAP"
FT TURN 153..157
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1KAP"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1AKL"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1KAP"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:1KAP"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1JIW"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:1KAP"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 438..444
FT /evidence="ECO:0007829|PDB:1KAP"
FT TURN 445..448
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 449..461
FT /evidence="ECO:0007829|PDB:1KAP"
FT STRAND 463..470
FT /evidence="ECO:0007829|PDB:1KAP"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:1KAP"
SQ SEQUENCE 479 AA; 50433 MW; 1865EA8F94232663 CRC64;
MSSNSLALKG RSDAYTQVDN FLHAYARGGD ELVNGHPSYT VDQAAEQILR EQASWQKAPG
DSVLTLSYSF LTKPNDFFNT PWKYVSDIYS LGKFSAFSAQ QQAQAKLSLQ SWSDVTNIHF
VDAGQGDQGD LTFGNFSSSV GGAAFAFLPD VPDALKGQSW YLINSSYSAN VNPANGNYGR
QTLTHEIGHT LGLSHPGDYN AGEGDPTYAD ATYAEDTRAY SVMSYWEEQN TGQDFKGAYS
SAPLLDDIAA IQKLYGANLT TRTGDTVYGF NSNTERDFYS ATSSSSKLVF SVWDAGGNDT
LDFSGFSQNQ KINLNEKALS DVGGLKGNVS IAAGVTVENA IGGSGSDLLI GNDVANVLKG
GAGNDILYGG LGADQLWGGA GADTFVYGDI AESSAAAPDT LRDFVSGQDK IDLSGLDAFV
NGGLVLQYVD AFAGKAGQAI LSYDAASKAG SLAIDFSGDA HADFAINLIG QATQADIVV
