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UniProtKB/Swiss-Prot entry P23694


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

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Entry information
Entry name PRZN_SERMA
Primary accession number P23694
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 75)
Name and origin of the protein
Protein name Serralysin [Precursor]
Synonyms EC 3.4.24.40
Extracellular metalloproteinase
Zinc proteinase
Gene name None
From
Serratia marcescens [TaxID: 615] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Serratia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SM6;
DOI=10.1007/BF00633854; PubMed=2274043 [NCBI, ExPASy, EBI, Israel, Japan]
Braunagel S.C., Benedik M.J.;
"The metalloprotease gene of Serratia marcescens strain SM6.";
Mol. Gen. Genet. 222:446-451(1990).
[2]
PROTEIN SEQUENCE OF 1-18, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
STRAIN=HR-3;
DOI=10.1007/s00284-005-0089-8; PubMed=16391997 [NCBI, ExPASy, EBI, Israel, Japan]
Tao K., Long Z., Liu K., Tao Y., Liu S.;
"Purification and properties of a novel insecticidal protein from the locust pathogen Serratia marcescens HR-3.";
Curr. Microbiol. 52:45-49(2006).
[3]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
DOI=10.1006/jmbi.1994.1576; PubMed=8089845 [NCBI, ExPASy, EBI, Israel, Japan]
Baumann U.;
"Crystal structure of the 50 kDa metallo protease from Serratia marcescens.";
J. Mol. Biol. 242:244-251(1994).
[4]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
DOI=10.1006/jmbi.1995.0249; PubMed=7752231 [NCBI, ExPASy, EBI, Israel, Japan]
Baumann U., Bauer M., Letoffe S., Delepelaire P., Wandersman C.;
"Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi.";
J. Mol. Biol. 248:653-661(1995).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Baumann U.;
Submitted (MAR-1997) to the PDB data bank.
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
X55521; CAA39137.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X55521; CAA39138.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X55521; CAA39139.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S12164; S12164.
3D structure databases
PDB
1AF0; X-ray; 1.80 A; A=17-487.[ExPASy / RCSB / EBI]
1SAT; X-ray; 1.75 A; A=17-487.[ExPASy / RCSB / EBI]
1SMP; X-ray; 2.30 A; A=17-487.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AF0; -.
1SAT; -.
1SMP; -.
ModBase P23694.
Protein family/group databases
MEROPS M10.051; -.
Ontologies
GO
GO:0005578; Cellular component: proteinaceous extracellular matrix (inferred from electronic annotation from InterPro).
GO:0005509; Molecular function: calcium ion binding (inferred from direct assay from UniProtKB).
GO:0004222; Molecular function: metalloendopeptidase activity (inferred from direct assay from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0009405; Biological process: pathogenesis (inferred from direct assay from UniProtKB).
GO:0006508; Biological process: proteolysis (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001343; Hemolysn_Ca-bd.
IPR001818; Pept_M10A_M12B.
IPR016294; Pept_M10B.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR013858; Peptidase_M10_C.
IPR003995; RTX_cytolytic_toxin_protA_bac.
Graphical view of domain structure.
Pfam PF00353; HemolysinCabind; 2.
PF00413; Peptidase_M10; 1.
PF08548; Peptidase_M10_C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001205; Peptidase_M10B; 1.
PRINTS PR00313; CABNDNGRPT.
PR01488; RTXTOXINA.
SMART SM00235; ZnMc; 1.
SMART graphical view of domain structure.
PROSITE PS00330; HEMOLYSIN_CALCIUM; 1.
PS00142; ZINC_PROTEASE; 1.
ProtoNet P23694.
Other
LinkHub P23694; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Protease; Repeat; Secreted; Toxin; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1    16  16      PRO_0000028693
CHAIN   17   487  471     Serralysin. PRO_0000028694
REPEAT   348   365  18     Hemolysin-type calcium-binding 1. 
REPEAT   366   383  18     Hemolysin-type calcium-binding 2. 
ACT_SITE   193   193         
METAL   192   192        Zinc; catalytic. 
METAL   196   196        Zinc; catalytic. 
METAL   202   202        Zinc; catalytic. 
METAL   232   232        Zinc; catalytic. 
METAL   269   269        Calcium 1; via carbonyl oxygen. 
METAL   271   271        Calcium 1; via carbonyl oxygen. 
METAL   273   273        Calcium 1. 
METAL   301   301        Calcium 1. 
METAL   303   303        Calcium 1; via carbonyl oxygen. 
METAL   304   304        Calcium 2; via carbonyl oxygen. 
METAL   306   306        Calcium 1. 
METAL   306   306        Calcium 2. 
METAL   343   343        Calcium 2; via carbonyl oxygen. 
METAL   345   345        Calcium 2. 
METAL   350   350        Calcium 3; via carbonyl oxygen. 
METAL   352   352        Calcium 3; via carbonyl oxygen. 
METAL   354   354        Calcium 3. 
METAL   359   359        Calcium 4; via carbonyl oxygen. 
METAL   361   361        Calcium 4; via carbonyl oxygen. 
METAL   363   363        Calcium 4. 
METAL   367   367        Calcium 3; via carbonyl oxygen. 
METAL   368   368        Calcium 5; via carbonyl oxygen. 
METAL   369   369        Calcium 3; via carbonyl oxygen. 
METAL   370   370        Calcium 5; via carbonyl oxygen. 
METAL   372   372        Calcium 3. 
METAL   372   372        Calcium 5. 
METAL   376   376        Calcium 4; via carbonyl oxygen. 
METAL   377   377        Calcium 6; via carbonyl oxygen. 
METAL   378   378        Calcium 4; via carbonyl oxygen. 
METAL   379   379        Calcium 6; via carbonyl oxygen. 
METAL   381   381        Calcium 4. 
METAL   381   381        Calcium 6. 
METAL   385   385        Calcium 5; via carbonyl oxygen. 
METAL   386   386        Calcium 7; via carbonyl oxygen. 
METAL   387   387        Calcium 5; via carbonyl oxygen. 
METAL   388   388        Calcium 7; via carbonyl oxygen. 
METAL   390   390        Calcium 5. 
METAL   390   390        Calcium 7. 
METAL   399   399        Calcium 6. 
METAL   406   406        Calcium 6. 
METAL   416   416        Calcium 7. 
CONFLICT   14    14        S -> E (in Ref. 2; AA sequence). 
HELIX   21    29  9      
TURN   30    32  3      
HELIX   48    55  8      
TURN   56    58  3      
STRAND   72    77  6      
HELIX   99   115  17      
STRAND   116   122  7      
STRAND   130   136  7      
STRAND   138   140  3      
STRAND   150   152  3      
STRAND   167   171  5      
HELIX   175   178  4      
TURN   180   182  3      
HELIX   184   198  15      
STRAND   203   205  3      
HELIX   215   217  3      
TURN   225   227  3      
HELIX   235   238  4      
HELIX   252   262  11      
TURN   266   269  4      
STRAND   274   276  3      
HELIX   284   286  3      
STRAND   297   299  3      
STRAND   307   309  3      
STRAND   318   320  3      
STRAND   326   328  3      
STRAND   336   338  3      
STRAND   346   348  3      
STRAND   355   357  3      
STRAND   364   366  3      
STRAND   373   375  3      
STRAND   382   384  3      
STRAND   391   393  3      
HELIX   397   400  4      
STRAND   406   408  3      
TURN   413   415  3      
STRAND   416   419  4      
HELIX   421   427  7      
STRAND   432   435  4      
STRAND   445   451  7      
TURN   452   455  4      
STRAND   456   461  6      
STRAND   470   477  8      
TURN   481   483  3      
STRAND   484   486  3      
Sequence information
Length: 487 AA [This is the length of the unprocessed precursor] Molecular weight: 52105 Da [This is the MW of the unprocessed precursor] CRC64: 8689FC84D83CAA2C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQSTKKAIEI TESSLAAATT GYDAVDDLLH YHERGNGIQI NGKDSFSNEQ AGLFITRENQ 

        70         80         90        100        110        120 
TWNGYKVFGQ PVKLTFSFPD YKFSSTNVAG DTGLSKFSAE QQQQAKLSLQ SWADVANITF 

       130        140        150        160        170        180 
TEVAAGQKAN ITFGNYSQDR PGHYDYGTQA YAFLPNTIWQ GQDLGGQTWY NVNQSNVKHP 

       190        200        210        220        230        240 
ATEDYGRQTF THEIGHALGL SHPGDYNAGE GNPTYNDVTY AEDTRQFSLM SYWSETNTGG 

       250        260        270        280        290        300 
DNGGHYAAAP LLDDIAAIQH LYGANPSTRT GDTVYGFNSN TGRDFLSTTS NSQKVIFAAW 

       310        320        330        340        350        360 
DAGGNDTFDF SGYTANQRIN LNEKSFSDVG GLKGNVSIAA GVTIENAIGG SGNDVIVGNA 

       370        380        390        400        410        420 
ANNVLKGGAG NDVLFGGGGA DELWGGAGKD IFVFSAASDS APGASDWIRD FQKGIDKIDL 

       430        440        450        460        470        480 
SFFNKEANSS DFIHFVDHFS GTAGEALLSY NASSNVTDLS VNIGGHQAPD FLVKIVGQVD 


VATDFIV 

P23694 in FASTA format

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