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Q03023 (APRA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serralysin
EC=3.4.24.40
Alternative name(s):
Alkaline metalloproteinase
Short name=AP
Gene names
Name:aprA
Ordered Locus Names:PA1249
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Preferential cleavage of bonds with hydrophobic residues in P1'. Ref.4

Cofactor

Binds 8 calcium ions per subunit.

Binds 1 zinc ion per subunit.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M10B family.

Contains 2 hemolysin-type calcium-binding repeats.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space

Inferred from electronic annotation. Source: InterPro

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 99
PRO_0000028681
Chain10 – 479470Serralysin
PRO_0000028682

Regions

Repeat341 – 35818Hemolysin-type calcium-binding 1
Repeat359 – 37618Hemolysin-type calcium-binding 2

Sites

Active site1861
Metal binding1851Zinc; catalytic
Metal binding1891Zinc; catalytic
Metal binding1951Zinc; catalytic
Metal binding2621Calcium 1; via carbonyl oxygen
Metal binding2641Calcium 1; via carbonyl oxygen
Metal binding2651Calcium 1
Metal binding2941Calcium 1
Metal binding2961Calcium 1; via carbonyl oxygen
Metal binding2971Calcium 2; via carbonyl oxygen
Metal binding2991Calcium 1
Metal binding2991Calcium 2
Metal binding3361Calcium 2; via carbonyl oxygen
Metal binding3381Calcium 2
Metal binding3431Calcium 3; via carbonyl oxygen
Metal binding3451Calcium 3; via carbonyl oxygen
Metal binding3471Calcium 3
Metal binding3521Calcium 4; via carbonyl oxygen
Metal binding3561Calcium 4
Metal binding3601Calcium 3; via carbonyl oxygen
Metal binding3611Calcium 5; via carbonyl oxygen
Metal binding3621Calcium 3; via carbonyl oxygen
Metal binding3631Calcium 5; via carbonyl oxygen
Metal binding3651Calcium 3
Metal binding3651Calcium 5
Metal binding3691Calcium 4; via carbonyl oxygen
Metal binding3701Calcium 6; via carbonyl oxygen
Metal binding3721Calcium 6; via carbonyl oxygen
Metal binding3741Calcium 4
Metal binding3741Calcium 6
Metal binding3781Calcium 5; via carbonyl oxygen
Metal binding3791Calcium 7; via carbonyl oxygen
Metal binding3801Calcium 5; via carbonyl oxygen
Metal binding3811Calcium 7; via carbonyl oxygen
Metal binding3831Calcium 5
Metal binding3831Calcium 7
Metal binding3991Calcium 6
Metal binding4091Calcium 7
Metal binding4571Calcium 8
Metal binding4591Calcium 8
Metal binding4631Calcium 8

Natural variations

Natural variant1271D → H in strain: IFO 3455.
Natural variant1761G → A in strain: IFO 3455.
Natural variant195 – 1973HPG → T in strain: IFO 3455.
Natural variant3501I → Y in strain: IFO 3455.
Natural variant388 – 3892GD → A in strain: IFO 3455.
Natural variant391 – 3922AE → SP in strain: IFO 3455.
Natural variant394 – 3963SAA → PPR in strain: IFO 3455.
Natural variant435 – 4395KAGQA → NAQG in strain: IFO 3455.
Natural variant4541I → V in strain: IFO 3455.
Natural variant4601A → R in strain: IFO 3455.
Natural variant4791V → L in strain: IFO 3455.

Secondary structure

1 ...................................................................................... 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03023 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 1865EA8F94232663

FASTA47950,433
        10         20         30         40         50         60 
MSSNSLALKG RSDAYTQVDN FLHAYARGGD ELVNGHPSYT VDQAAEQILR EQASWQKAPG 

        70         80         90        100        110        120 
DSVLTLSYSF LTKPNDFFNT PWKYVSDIYS LGKFSAFSAQ QQAQAKLSLQ SWSDVTNIHF 

       130        140        150        160        170        180 
VDAGQGDQGD LTFGNFSSSV GGAAFAFLPD VPDALKGQSW YLINSSYSAN VNPANGNYGR 

       190        200        210        220        230        240 
QTLTHEIGHT LGLSHPGDYN AGEGDPTYAD ATYAEDTRAY SVMSYWEEQN TGQDFKGAYS 

       250        260        270        280        290        300 
SAPLLDDIAA IQKLYGANLT TRTGDTVYGF NSNTERDFYS ATSSSSKLVF SVWDAGGNDT 

       310        320        330        340        350        360 
LDFSGFSQNQ KINLNEKALS DVGGLKGNVS IAAGVTVENA IGGSGSDLLI GNDVANVLKG 

       370        380        390        400        410        420 
GAGNDILYGG LGADQLWGGA GADTFVYGDI AESSAAAPDT LRDFVSGQDK IDLSGLDAFV 

       430        440        450        460        470 
NGGLVLQYVD AFAGKAGQAI LSYDAASKAG SLAIDFSGDA HADFAINLIG QATQADIVV

« Hide

References

« Hide 'large scale' references
[1]"Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways."
Duong F., Lazdunski A., Cami B., Murgier M.
Gene 121:47-54(1992) [PubMed: 1427098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete nucleotide sequence of the structural gene for alkaline proteinase from Pseudomonas aeruginosa IFO 3455."
Okuda K., Morihara K., Atsumi Y., Takeuchi H., Kawamoto S., Kawasaki H., Suzuki K., Fukushima J.
Infect. Immun. 58:4083-4088(1990) [PubMed: 2123832] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NBRC 13130 / JCM 20134.
[3]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[4]"On the specificity of Pseudomonas aeruginosa alkaline proteinase with synthetic peptides."
Morihara K., Tsuzuki H., Oka T.
Biochim. Biophys. Acta 309:414-429(1973) [PubMed: 4199986] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
[5]"Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif."
Baumann U., Wu S., Flaherty K.M., McKay D.B.
EMBO J. 12:3357-3364(1993) [PubMed: 8253063] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[6]"Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding."
Miyatake H., Hata Y., Fujii T., Hamada K., Morihara K., Katsube Y.
J. Biochem. 118:474-479(1995) [PubMed: 8690704] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: ATCC 21636 / NBRC 3080.
[7]"Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond."
Hege T., Feltzer R.E., Gray R.D., Baumann U.
J. Biol. Chem. 276:35087-35092(2001) [PubMed: 11445573] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH PROTEASE INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X64558 Genomic DNA. Translation: CAA45858.1.
AE004091 Genomic DNA. Translation: AAG04638.1.
PIRA41463.
S26699.
RefSeqNP_249940.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKLX-ray2.00A10-479[»]
1JIWX-ray1.74P10-479[»]
1KAPX-ray1.64P1-479[»]
ProteinModelPortalQ03023.
SMRQ03023. Positions 10-479.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-204154.

Protein family/group databases

MEROPSM10.056.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID881248.
GenomeReviewsGene locus PA1249 in contig AE004091_GR.
KEGGpae:PA1249.
PATRIC19836822. VBIPseAer58763_1297.

Organism-specific databases

PseudoCAPPA1249.

Phylogenomic databases

HOGENOMHBG598843.
OMAINSSYSA.
ProtClustDBCLSK866434.

Enzyme and pathway databases

BioCycPAER208964:PA1249-MONOMER.

Family and domain databases

InterProIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR024079. MetalloPept_cat_dom.
IPR016294. Pept_M10B.
IPR013858. Peptidase_M10B_C.
IPR006026. Peptidase_Metallo.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
Gene3DG3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
PfamPF00353. HemolysinCabind. 3 hits.
PF08548. Peptidase_M10_C. 1 hit.
[Graphical view]
PIRSFPIRSF001205. Peptidase_M10B. 1 hit.
SMARTSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF51120. Serralysn_like_C. 1 hit.
PROSITEPS00330. HEMOLYSIN_CALCIUM. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPRA_PSEAE
AccessionPrimary (citable) accession number: Q03023
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents