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P07268 (PRZN_SERME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. 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):
Extracellular metalloproteinase
Serratiopeptidase
Short name=Serrapeptase
Short name=Serrapeptidase
Zinc proteinase
OrganismSerratia marcescens (strain ATCC 21074 / E-15)
Taxonomic identifier617 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Naturally present in the silkworm intestine and allows the emerging moth to dissolve its cocoon.

Catalytic activity

Preferential cleavage of bonds with hydrophobic residues in P1'.

Cofactor

Binds 7 calcium ions per subunit.

Binds 1 zinc ion per subunit.

Subcellular location

Secreted.

Miscellaneous

The Gly-rich repeats may be important in the extracellular secretion of this metalloprotease.

In Japan this enzyme, isolated from a Serratia strain presents in the gut of silkworms, is used as a food supplement because it is reported to induces fibrinolytic, anti-inflammatory and anti-edemic (prevents swelling and fluid retention) activity in a number of tissues.

Sequence similarities

Belongs to the peptidase M10B family.

Contains 2 hemolysin-type calcium-binding repeats.

Sequence caution

The sequence CAA27738.1 differs from that shown. Reason: Frameshift at positions 350 and 355.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular matrix

Inferred from electronic annotation. Source: InterPro

extracellular 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 – 1616
PRO_0000028695
Chain17 – 487471Serralysin
PRO_0000028696

Regions

Repeat348 – 36518Hemolysin-type calcium-binding 1
Repeat366 – 38318Hemolysin-type calcium-binding 2

Sites

Active site1931
Metal binding1921Zinc; catalytic
Metal binding1961Zinc; catalytic
Metal binding2021Zinc; catalytic
Metal binding2321Zinc; catalytic
Metal binding2691Calcium 1; via carbonyl oxygen
Metal binding2711Calcium 1; via carbonyl oxygen
Metal binding2731Calcium 1
Metal binding3011Calcium 1
Metal binding3031Calcium 1; via carbonyl oxygen
Metal binding3041Calcium 2; via carbonyl oxygen
Metal binding3061Calcium 1
Metal binding3061Calcium 2
Metal binding3431Calcium 2; via carbonyl oxygen
Metal binding3451Calcium 2
Metal binding3501Calcium 3; via carbonyl oxygen
Metal binding3521Calcium 3; via carbonyl oxygen
Metal binding3541Calcium 3
Metal binding3591Calcium 4; via carbonyl oxygen
Metal binding3611Calcium 4; via carbonyl oxygen
Metal binding3631Calcium 4
Metal binding3671Calcium 3; via carbonyl oxygen
Metal binding3681Calcium 5; via carbonyl oxygen
Metal binding3691Calcium 3; via carbonyl oxygen
Metal binding3721Calcium 3
Metal binding3721Calcium 5
Metal binding3761Calcium 4; via carbonyl oxygen
Metal binding3771Calcium 6; via carbonyl oxygen
Metal binding3781Calcium 4; via carbonyl oxygen
Metal binding3791Calcium 6; via carbonyl oxygen
Metal binding3811Calcium 4
Metal binding3811Calcium 6
Metal binding3851Calcium 5; via carbonyl oxygen
Metal binding3861Calcium 7; via carbonyl oxygen
Metal binding3871Calcium 5; via carbonyl oxygen
Metal binding3881Calcium 7; via carbonyl oxygen
Metal binding3901Calcium 5
Metal binding3901Calcium 7
Metal binding3991Calcium 6
Metal binding4061Calcium 6
Metal binding4161Calcium 7

Secondary structure

1 ........................................................................................ 487
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07268 [UniParc].

Last modified June 20, 2003. Version 2.
Checksum: 270A315CADD568C3

FASTA48752,235
        10         20         30         40         50         60 
MQSTKKAIEI TESNFAAATT 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 GNPTYRDVTY AEDTRQFSLM SYWSETNTGG 

       250        260        270        280        290        300 
DNGGHYAAAP LLDDIAAIQH LYGANLSTRT 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 
SFFNKEAQSS DFIHFVDHFS GAAGEALLSY NASNNVTDLS VNIGGHQAPD FLVKIVGQVD 


VATDFIV

« Hide

References

[1]"Cloning and sequencing of Serratia protease gene."
Nakahama K., Yoshimura K., Marumoto R., Kikuchi M., Lee I.S., Hase T., Matsubara H.
Nucleic Acids Res. 14:5843-5855(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Serratia protease. Amino acid sequences of both termini, the 53 residues in the middle region containing the sole methionine residue, and a probable zinc-binding region."
Lee I.S., Wakabayashi S., Miyata K., Tomoda K., Yoneda M., Kangawa K., Minamino N., Matsuo H., Matsubara H.
J. Biochem. 96:1409-1418(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-34 AND 179-269.
[3]"Crystal structure of Serratia protease, a zinc-dependent proteinase from Serratia sp. E-15, containing a beta-sheet coil motif at 2.0-A resolution."
Hamada K., Hata Y., Katsuya Y., Hiramatsu H., Fujiwara T., Katsube Y.
J. Biochem. 119:844-851(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-487.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X04127 Genomic DNA. Translation: CAA27738.1. Frameshift.
PIRHYSE15. A23596.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SRPX-ray2.00A17-487[»]
ProteinModelPortalP07268.
SMRP07268. Positions 20-487.
ModBaseSearch...

Protein family/group databases

MEROPSM10.051.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR016294. Pept_M10B.
IPR013858. Peptidase_M10B_C.
IPR006026. Peptidase_Metallo.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamPF00353. HemolysinCabind. 4 hits.
PF00413. Peptidase_M10. 1 hit.
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...

Other

EvolutionaryTraceP07268.

Entry information

Entry namePRZN_SERME
AccessionPrimary (citable) accession number: P07268
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 20, 2003
Last modified: April 3, 2013
This is version 107 of the entry and version 2 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

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