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P00778 (PRLA_LYSEN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 107. Feed History...

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

Names and origin

Protein namesRecommended name:
Alpha-lytic protease

EC=3.4.21.12
Alternative name(s):
Alpha-lytic endopeptidase
Gene names
Name:alpha-LP
OrganismLysobacter enzymogenes
Taxonomic identifier69 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeLysobacter

Protein attributes

Sequence length397 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: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins.

Sequence similarities

Belongs to the peptidase S1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 199175
PRO_0000026907
Chain200 – 397198Alpha-lytic protease
PRO_0000026908

Sites

Active site2351Charge relay system By similarity
Active site2621Charge relay system By similarity
Active site3421Charge relay system By similarity

Amino acid modifications

Disulfide bond216 ↔ 236
Disulfide bond300 ↔ 310
Disulfide bond336 ↔ 369

Experimental info

Sequence conflict1711E → D in AAA74111. Ref.3

Secondary structure

.................................................................... 397
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00778 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: 267FE6EBF57F33CB

FASTA39741,077
        10         20         30         40         50         60 
MYVSNHRSRR VARVSVSCLV AALAAMSCGA ALAADQVDPQ LKFAMQRDLG IFPTQLPQYL 

        70         80         90        100        110        120 
QTEKLARTQA AAIEREFGAQ FAGSWIERNE DGSFKLVAAT SGARKSSTLG GVEVRNVRYS 

       130        140        150        160        170        180 
LKQLQSAMEQ LDAGANARVK GVSKPLDGVQ SWYVDPRSNA VVVKVDDGAT EAGVDFVALS 

       190        200        210        220        230        240 
GADSAQVRIE SSPGKLQTTA NIVGGIEYSI NNASLCSVGF SVTRGATKGF VTAGHCGTVN 

       250        260        270        280        290        300 
ATARIGGAVV GTFAARVFPG NDRAWVSLTS AQTLLPRVAN GSSFVTVRGS TEAAVGAAVC 

       310        320        330        340        350        360 
RSGRTTGYQC GTITAKNVTA NYAEGAVRGL TQGNACMGRG DSGGSWITSA GQAQGVMSGG 

       370        380        390 
NVQSNGNNCG IPASQRSSLF ERLQPILSQY GLSLVTG 

« Hide

References

[1]"The alpha-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes."
Epstein D.M., Wensink P.C.
J. Biol. Chem. 263:16586-16590(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235.
[2]Epstein D.M.
Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Molecular analysis of the gene encoding alpha-lytic protease: evidence for a preproenzyme."
Silen J.L., McGrath C.N., Smith K.R., Agard D.A.
Gene 69:237-244(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235.
[4]"Priaary structure of alpha-lytic protease: a bacterial homologue of the pancreatic serine proteases."
Olson M.O.J., Nagabhushan N., Dzwiniel M., Smillie L.B., Whitaker D.R.
Nature 228:438-442(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 199-396.
Strain: ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235.
[5]"Molecular structure of the alpha-lytic protease from Myxobacter 495 at 2.8-A resolution."
Brayer G.D., Delbaere L.T.J., James M.N.G.
J. Mol. Biol. 131:743-775(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]"Refined structure of alpha-lytic protease at 1.7-A resolution. Analysis of hydrogen bonding and solvent structure."
Fujinaga M., Delbaere L.T.J., Brayer G.D., James M.N.G.
J. Mol. Biol. 184:479-502(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[7]"Pro region C-terminus: protease active site interactions are critical in catalyzing the folding of alpha-lytic protease."
Peters R.J., Shiau A.K., Sohl J.L., Anderson D.E., Tang G., Silen J.L., Agard D.A.
Biochemistry 37:12058-12067(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Strain: ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235.
[8]"Structure of alpha-lytic protease complexed with its pro region."
Sauter N.K., Mau T., Rader S.D., Agard D.A.
Nat. Struct. Biol. 5:945-950(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04052 Genomic DNA. Translation: AAA25409.1.
M22763 Genomic DNA. Translation: AAA74111.1.
PIRTRYXB4. A31772.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOQX-ray2.10A200-397[»]
1GBAX-ray2.15A200-397[»]
1GBBX-ray2.15A200-397[»]
1GBCX-ray2.20A200-397[»]
1GBDX-ray2.20A200-397[»]
1GBEX-ray2.30A200-397[»]
1GBFX-ray2.15A200-397[»]
1GBHX-ray2.20A200-397[»]
1GBIX-ray2.30A200-397[»]
1GBJX-ray2.00A200-397[»]
1GBKX-ray2.13A200-397[»]
1GBLX-ray2.15A200-397[»]
1GBMX-ray2.28A200-397[»]
1P01X-ray2.00A200-397[»]
1P02X-ray2.00A200-397[»]
1P03X-ray2.15A200-397[»]
1P04X-ray2.55A200-397[»]
1P05X-ray2.10A200-397[»]
1P06X-ray2.34A200-397[»]
1P09X-ray2.20A200-397[»]
1P10X-ray2.25A200-397[»]
1P11X-ray1.93E200-397[»]
1P12X-ray1.90E200-397[»]
1QQ4X-ray1.20A200-397[»]
1QRWX-ray1.20A200-397[»]
1QRXX-ray1.60A200-397[»]
1SSXX-ray0.83A200-397[»]
1TALX-ray1.50A200-397[»]
2ALPX-ray1.70A200-397[»]
2H5CX-ray0.82A200-397[»]
2H5DX-ray0.90A200-397[»]
2LPRX-ray2.25A200-397[»]
2PROX-ray3.00A/B/C34-199[»]
2ULLX-ray1.50A200-397[»]
3LPRX-ray2.15A200-397[»]
3M7TX-ray1.55A200-397[»]
3M7UX-ray1.05A200-397[»]
3PROX-ray1.80A/B200-397[»]
C/D34-199[»]
3QGJX-ray1.30A/C200-397[»]
3URCX-ray1.10A200-397[»]
3URDX-ray1.08A200-397[»]
3UREX-ray1.49A/B200-397[»]
4PROX-ray2.40A/B200-397[»]
C/D34-199[»]
5LPRX-ray2.13A200-397[»]
6LPRX-ray2.10A200-397[»]
7LPRX-ray2.05A200-397[»]
8LPRX-ray2.25A200-397[»]
9LPRX-ray2.20A200-397[»]
ProteinModelPortalP00778.
SMRP00778. Positions 38-397.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR004236. Pept_S1_alpha_lytic.
IPR001316. Pept_S1A_streptogrisin.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF02983. Pro_Al_protease. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001134. Streptogrisin. 1 hit.
PRINTSPR00861. ALYTICPTASE.
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00778.

Entry information

Entry namePRLA_LYSEN
AccessionPrimary (citable) accession number: P00778
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references