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UniProtKB/Swiss-Prot entry P00778


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRLA_LYSEN
Primary accession number P00778
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on February 1, 1996 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 83)
Name and origin of the protein
Protein name Alpha-lytic protease [Precursor]
Synonyms EC 3.4.21.12
Alpha-lytic endopeptidase
Gene name
Name: alpha-LP
From
Lysobacter enzymogenes [TaxID: 69] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Lysobacter.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235;
PubMed=3053694 [NCBI, ExPASy, EBI, Israel, Japan]
Epstein D.M., Wensink P.C.;
"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.";
J. Biol. Chem. 263:16586-16590(1988).
[2]
SEQUENCE REVISION.
Epstein D.M.;
Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235;
DOI=10.1016/0378-1119(88)90434-9; PubMed=3234766 [NCBI, ExPASy, EBI, Israel, Japan]
Silen J.L., McGrath C.N., Smith K.R., Agard D.A.;
"Molecular analysis of the gene encoding alpha-lytic protease: evidence for a preproenzyme.";
Gene 69:237-244(1988).
[4]
PROTEIN SEQUENCE OF 199-396.
STRAIN=ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235;
DOI=10.1038/228438a0; PubMed=5482494 [NCBI, ExPASy, EBI, Israel, Japan]
Olson M.O.J., Nagabhushan N., Dzwiniel M., Smillie L.B., Whitaker D.R.;
"Priaary structure of alpha-lytic protease: a bacterial homologue of the pancreatic serine proteases.";
Nature 228:438-442(1970).
[5]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1016/0022-2836(79)90200-6; PubMed=117110 [NCBI, ExPASy, EBI, Israel, Japan]
Brayer G.D., Delbaere L.T.J., James M.N.G.;
"Molecular structure of the alpha-lytic protease from Myxobacter 495 at 2.8-A resolution.";
J. Mol. Biol. 131:743-775(1979).
[6]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
DOI=10.1016/0022-2836(85)90296-7; PubMed=3900416 [NCBI, ExPASy, EBI, Israel, Japan]
Fujinaga M., Delbaere L.T.J., Brayer G.D., James M.N.G.;
"Refined structure of alpha-lytic protease at 1.7-A resolution. Analysis of hydrogen bonding and solvent structure.";
J. Mol. Biol. 184:479-502(1985).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
STRAIN=ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235;
DOI=10.1021/bi980883v; PubMed=9724517 [NCBI, ExPASy, EBI, Israel, Japan]
Peters R.J., Shiau A.K., Sohl J.L., Anderson D.E., Tang G., Silen J.L., Agard D.A.;
"Pro region C-terminus: protease active site interactions are critical in catalyzing the folding of alpha-lytic protease.";
Biochemistry 37:12058-12067(1998).
[8]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1038/2919; PubMed=9808037 [NCBI, ExPASy, EBI, Israel, Japan]
Sauter N.K., Mau T., Rader S.D., Agard D.A.;
"Structure of alpha-lytic protease complexed with its pro region.";
Nat. Struct. Biol. 5:945-950(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J04052; AAA25409.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22763; AAA74111.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31772; TRYXB4.
3D structure databases
PDB
1BOQ; X-ray; 2.10 A; A=200-397.[ExPASy / RCSB / EBI]
1GBA; X-ray; 2.15 A; A=200-397.[ExPASy / RCSB / EBI]
1GBB; X-ray; 2.15 A; A=200-397.[ExPASy / RCSB / EBI]
1GBC; X-ray; 2.20 A; A=200-397.[ExPASy / RCSB / EBI]
1GBD; X-ray; 2.20 A; A=200-397.[ExPASy / RCSB / EBI]
1GBE; X-ray; 2.30 A; A=200-397.[ExPASy / RCSB / EBI]
1GBF; X-ray; 2.15 A; A=200-397.[ExPASy / RCSB / EBI]
1GBH; X-ray; 2.20 A; A=200-397.[ExPASy / RCSB / EBI]
1GBI; X-ray; 2.30 A; A=200-397.[ExPASy / RCSB / EBI]
1GBJ; X-ray; 2.00 A; A=200-397.[ExPASy / RCSB / EBI]
1GBK; X-ray; 2.13 A; A=200-397.[ExPASy / RCSB / EBI]
1GBL; X-ray; 2.15 A; A=200-397.[ExPASy / RCSB / EBI]
1GBM; X-ray; 2.28 A; A=200-397.[ExPASy / RCSB / EBI]
1P01; X-ray; 2.00 A; A=200-397.[ExPASy / RCSB / EBI]
1P02; X-ray; 2.00 A; A=200-397.[ExPASy / RCSB / EBI]
1P03; X-ray; 2.15 A; A=200-397.[ExPASy / RCSB / EBI]
1P04; X-ray; 2.55 A; A=200-397.[ExPASy / RCSB / EBI]
1P05; X-ray; 2.10 A; A=200-397.[ExPASy / RCSB / EBI]
1P06; X-ray; 2.34 A; A=200-397.[ExPASy / RCSB / EBI]
1P09; X-ray; 2.20 A; A=200-397.[ExPASy / RCSB / EBI]
1P10; X-ray; 2.25 A; A=200-397.[ExPASy / RCSB / EBI]
1P11; X-ray; 1.93 A; E=200-397.[ExPASy / RCSB / EBI]
1P12; X-ray; 1.90 A; E=200-397.[ExPASy / RCSB / EBI]
1QQ4; X-ray; 1.20 A; A=200-397.[ExPASy / RCSB / EBI]
1QRW; X-ray; 1.20 A; A=200-397.[ExPASy / RCSB / EBI]
1QRX; X-ray; 1.60 A; A=200-397.[ExPASy / RCSB / EBI]
1SSX; X-ray; 0.83 A; A=200-397.[ExPASy / RCSB / EBI]
1TAL; X-ray; 1.50 A; A=200-397.[ExPASy / RCSB / EBI]
2ALP; X-ray; 1.70 A; A=200-397.[ExPASy / RCSB / EBI]
2H5C; X-ray; 0.82 A; A=200-397.[ExPASy / RCSB / EBI]
2H5D; X-ray; 0.90 A; A=200-397.[ExPASy / RCSB / EBI]
2LPR; X-ray; 2.25 A; A=200-397.[ExPASy / RCSB / EBI]
2PRO; X-ray; 3.00 A; A/B/C=34-199.[ExPASy / RCSB / EBI]
2ULL; X-ray; 1.50 A; A=200-397.[ExPASy / RCSB / EBI]
3LPR; X-ray; 2.15 A; A=200-397.[ExPASy / RCSB / EBI]
3PRO; X-ray; 1.80 A; A/B=200-397, C/D=34-199.[ExPASy / RCSB / EBI]
4PRO; X-ray; 2.40 A; A/B=200-397, C/D=34-199.[ExPASy / RCSB / EBI]
5LPR; X-ray; 2.13 A; A=200-397.[ExPASy / RCSB / EBI]
6LPR; X-ray; 2.10 A; A=200-397.[ExPASy / RCSB / EBI]
7LPR; X-ray; 2.05 A; A=200-397.[ExPASy / RCSB / EBI]
8LPR; X-ray; 2.25 A; A=200-397.[ExPASy / RCSB / EBI]
9LPR; X-ray; 2.20 A; A=200-397.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BOQ; -.
1GBA; -.
1GBB; -.
1GBC; -.
1GBD; -.
1GBE; -.
1GBF; -.
1GBH; -.
1GBI; -.
1GBJ; -.
1GBK; -.
1GBL; -.
1GBM; -.
1P01; -.
1P02; -.
1P03; -.
1P04; -.
1P05; -.
1P06; -.
1P09; -.
1P10; -.
1P11; -.
1P12; -.
1QQ4; -.
1QRW; -.
1QRX; -.
1SSX; -.
1TAL; -.
2ALP; -.
2H5C; -.
2H5D; -.
2LPR; -.
2PRO; -.
2ULL; -.
3LPR; -.
3PRO; -.
4PRO; -.
5LPR; -.
6LPR; -.
7LPR; -.
8LPR; -.
9LPR; -.
ModBase P00778.
Protein family/group databases
MEROPS S01.268; -.
Family and domain databases
InterPro IPR004236; Pept_S1_alpha_lytic.
IPR001316; Pept_S1A_streptogrisin.
IPR001254; Peptidase_S1_S6.
Graphical view of domain structure.
Pfam PF02983; Pro_Al_protease; 2.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001134; Streptogrisin; 1.
PRINTS PR00861; ALYTICPTASE.
PROSITE PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
BLOCKS P00778.
ProtoNet P00778.
Other
SWISS-3DIMAGE P00778.
LinkHub P00778; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Hydrolase; Protease; Serine protease; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    24  24     Potential. 
PROPEP   25   199  175      PRO_0000026907
CHAIN   200   397  198     Alpha-lytic protease. PRO_0000026908
ACT_SITE   235   235         
ACT_SITE   262   262         
ACT_SITE   342   342         
DISULFID   216   236         
DISULFID   300   310         
DISULFID   336   369         
CONFLICT   171   171        E -> D (in Ref. 3; AAA74111). 
HELIX   40    49  10      
HELIX   53    55  3      
HELIX   56    77  22      
HELIX   78    80  3      
STRAND   81    88  8      
STRAND   94   103  10      
STRAND   112   116  5      
HELIX   121   136  16      
STRAND   149   155  7      
HELIX   156   158  3      
STRAND   160   166  7      
HELIX   170   180  11      
TURN   184   186  3      
STRAND   187   195  9      
STRAND   201   204  4      
STRAND   207   210  4      
TURN   211   213  3      
STRAND   214   217  4      
STRAND   220   224  5      
STRAND   227   232  6      
HELIX   234   236  3      
STRAND   242   245  4      
STRAND   248   257  10      
STRAND   259   261  3      
STRAND   263   268  6      
STRAND   272   280  9      
STRAND   283   286  4      
STRAND   298   303  6      
TURN   304   306  3      
STRAND   307   322  16      
STRAND   325   333  9      
STRAND   345   347  3      
STRAND   352   360  9      
STRAND   366   368  3      
HELIX   373   375  3      
STRAND   378   382  5      
HELIX   383   390  8      
Sequence information
Length: 397 AA [This is the length of the unprocessed precursor] Molecular weight: 41077 Da [This is the MW of the unprocessed precursor] CRC64: 267FE6EBF57F33CB [This is a checksum on the sequence]
        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 

P00778 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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