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P23694 (PRZN_SERMA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 91. 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
Zinc proteinase
OrganismSerratia marcescens
Taxonomic identifier615 [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

Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death. Ref.2

Catalytic activity

Preferential cleavage of bonds with hydrophobic residues in P1'. Ref.2

Cofactor

Binds 7 calcium ions per subunit. Ref.2

Binds 1 zinc ion per subunit. Ref.2

Subcellular location

Secreted.

Miscellaneous

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

Sequence similarities

Belongs to the peptidase M10B family.

Contains 2 hemolysin-type calcium-binding repeats.

Sequence caution

The sequence CAA39138.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA39139.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from direct assay Ref.2. Source: UniProtKB

proteolysis

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular componentextracellular matrix

Inferred from electronic annotation. Source: InterPro

extracellular space

Inferred from electronic annotation. Source: InterPro

   Molecular functioncalcium ion binding

Inferred from direct assay Ref.2. Source: UniProtKB

metalloendopeptidase activity

Inferred from direct assay Ref.2. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1616
PRO_0000028693
Chain17 – 487471Serralysin
PRO_0000028694

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 binding3701Calcium 5; 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

Experimental info

Sequence conflict141S → E AA sequence Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P23694 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 8689FC84D83CAA2C

FASTA48752,105
        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

« Hide

References

[1]"The metalloprotease gene of Serratia marcescens strain SM6."
Braunagel S.C., Benedik M.J.
Mol. Gen. Genet. 222:446-451(1990) [PubMed: 2274043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SM6.
[2]"Purification and properties of a novel insecticidal protein from the locust pathogen Serratia marcescens HR-3."
Tao K., Long Z., Liu K., Tao Y., Liu S.
Curr. Microbiol. 52:45-49(2006) [PubMed: 16391997] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-18, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
Strain: HR-3.
[3]"Crystal structure of the 50 kDa metallo protease from Serratia marcescens."
Baumann U.
J. Mol. Biol. 242:244-251(1994) [PubMed: 8089845] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
[4]"Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi."
Baumann U., Bauer M., Letoffe S., Delepelaire P., Wandersman C.
J. Mol. Biol. 248:653-661(1995) [PubMed: 7752231] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
[5]Baumann U.
Submitted (MAR-1997) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X55521 Genomic DNA. Translation: CAA39137.1.
X55521 Genomic DNA. Translation: CAA39138.1. Different initiation.
X55521 Genomic DNA. Translation: CAA39139.1. Different initiation.
PIRS12164.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AF0X-ray1.80A17-487[»]
1SATX-ray1.75A17-487[»]
1SMPX-ray2.30A17-487[»]
ProteinModelPortalP23694.
SMRP23694. Positions 20-487.
ModBaseSearch...

Protein family/group databases

MEROPSM10.051.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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]
Gene3DG3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
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...

Entry information

Entry namePRZN_SERMA
AccessionPrimary (citable) accession number: P23694
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: September 21, 2011
This is version 91 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