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Reviewed, UniProtKB/Swiss-Prot P05458 (PTRA_ECOLI)

Last modified June 16, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Protease 3
    EC=3.4.24.55
Alternative name(s):
    Protease III
    Pitrilysin
    Protease pi
Gene names
Name: ptrA
Synonyms: ptr
Ordered Locus Names: b2821, JW2789
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length962 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin.

Catalytic activity

Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on other substrates of Mw less than 7 kDa such as insulin and glucagon.

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Monomer.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the peptidase M16 family.

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Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMagnesium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 962939Protease 3
PRO_0000026758

Sites

Active site911Proton acceptor Ref.6 Ref.7
Metal binding881Zinc Ref.6
Metal binding921Zinc Ref.6
Metal binding1691Zinc

Experimental info

Mutagenesis881H → R: Loss of activity and of Zn-binding.
Mutagenesis911E → Q: Loss of activity.
Mutagenesis921H → R: Loss of activity and of Zn-binding.
Mutagenesis1621E → Q: 20% loss of activity.
Mutagenesis1691E → Q: Loss of activity and of Zn-binding.
Mutagenesis2041E → Q: No loss of activity.
Sequence conflict277 – 2848IIIHYVPA → HYHSLRPW in AAA24436. Ref.5

Secondary structure

1 ................................................................................................................................................... 962
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P05458-1 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 0558C68C2F1A0540

FASTA962107,708
        10         20         30         40         50         60 
MPRSTWFKAL LLLVALWAPL SQAETGWQPI QETIRKSDKD NRQYQAIRLD NGMVVLLVSD 

        70         80         90        100        110        120 
PQAVKSLSAL VVPVGSLEDP EAYQGLAHYL EHMSLMGSKK YPQADSLAEY LKMHGGSHNA 

       130        140        150        160        170        180 
STAPYRTAFY LEVENDALPG AVDRLADAIA EPLLDKKYAE RERNAVNAEL TMARTRDGMR 

       190        200        210        220        230        240 
MAQVSAETIN PAHPGSKFSG GNLETLSDKP GNPVQQALKD FHEKYYSANL MKAVIYSNKP 

       250        260        270        280        290        300 
LPELAKMAAD TFGRVPNKES KKPEITVPVV TDAQKGIIIH YVPALPRKVL RVEFRIDNNS 

       310        320        330        340        350        360 
AKFRSKTDEL ITYLIGNRSP GTLSDWLQKQ GLVEGISANS DPIVNGNSGV LAISASLTDK 

       370        380        390        400        410        420 
GLANRDQVVA AIFSYLNLLR EKGIDKQYFD ELANVLDIDF RYPSITRDMD YVEWLADTMI 

       430        440        450        460        470        480 
RVPVEHTLDA VNIADRYDAK AVKERLAMMT PQNARIWYIS PKEPHNKTAY FVDAPYQVDK 

       490        500        510        520        530        540 
ISAQTFADWQ KKAADIALSL PELNPYIPDD FSLIKSEKKY DHPELIVDES NLRVVYAPSR 

       550        560        570        580        590        600 
YFASEPKADV SLILRNPKAM DSARNQVMFA LNDYLAGLAL DQLSNQASVG GISFSTNANN 

       610        620        630        640        650        660 
GLMVNANGYT QRLPQLFQAL LEGYFSYTAT EDQLEQAKSW YNQMMDSAEK GKAFEQAIMP 

       670        680        690        700        710        720 
AQMLSQVPYF SRDERRKILP SITLKEVLAY RDALKSGARP EFMVIGNMTE AQATTLARDV 

       730        740        750        760        770        780 
QKQLGADGSE WCRNKDVVVD KKQSVIFEKA GNSTDSALAA VFVPTGYDEY TSSAYSSLLG 

       790        800        810        820        830        840 
QIVQPWFYNQ LRTEEQLGYA VFAFPMSVGR QWGMGFLLQS NDKQPSFLWE RYKAFFPTAE 

       850        860        870        880        890        900 
AKLRAMKPDE FAQIQQAVIT QMLQAPQTLG EEASKLSKDF DRGNMRFDSR DKIVAQIKLL 

       910        920        930        940        950        960 
TPQKLADFFH QAVVEPQGMA ILSQISGSQN GKAEYVHPEG WKVWENVSAL QQTMPLMSEK 


NE

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References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III."
Finch P.W., Wilson R.E., Brown K., Hickson I.D., Emmerson P.T.
Nucleic Acids Res. 14:7695-7703(1986) [PubMed: 3534791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Complete nucleotide sequence of the Escherichia coli recB gene."
Finch P.W., Storey A., Chapman K.E., Brown K., Hickson I.D., Emmerson P.T.
Nucleic Acids Res. 14:8573-8582(1986) [PubMed: 3537960] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 853-962.
[5]"Analysis of the regulatory region of the protease III (ptr) gene of Escherichia coli K-12."
Claverie-Martin F., Diaz-Torres M.R., Kushner S.R.
Gene 54:185-195(1987) [PubMed: 3308636] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296.
Strain: K12.
[6]"An unusual active site identified in a family of zinc metalloendopeptidases."
Becker A.B., Roth R.A.
Proc. Natl. Acad. Sci. U.S.A. 89:3835-3839(1992) [PubMed: 1570301] [Abstract]
Cited for: MUTAGENESIS, ACTIVE SITE.
[7]"Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes."
Becker A.B., Roth R.A.
Biochem. J. 292:137-142(1993) [PubMed: 8099278] [Abstract]
Cited for: MUTAGENESIS, ACTIVE SITE.

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Cross-references

Sequence databases

X04581 Genomic DNA. Translation: CAA28249.1.
U29581 Genomic DNA. Translation: AAB40468.1.
U00096 Genomic DNA. Translation: AAC75860.1.
AP009048 Genomic DNA. Translation: BAE76890.1.
X06227 Genomic DNA. Translation: CAA29576.1.
M17095 Genomic DNA. Translation: AAA24436.1.
PIRSNECPI. F65064.
RefSeqAP_003384.1.
NP_417298.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1Q2LX-ray2.20A24-962[»]
ModBaseSearch...

Protein family/group databases

MEROPSM16.001.

2-D gel databases

ECO2DBASEG095.0. 6TH EDITION.

Genome annotation databases

GeneID947284.
GenomeReviewsGene locus JW2789 in contig AP009048_GR.
Gene locus b2821 in contig U00096_GR.
KEGGecj:JW2789.
eco:b2821.

Organism-specific databases

EchoBASEEB0779.
EcoGeneEG10786. ptrA.
CMRSearch...

Phylogenomic databases

HOGENOMP05458.
OMAP05458. YFSSEPK.

Enzyme and pathway databases

BioCycEcoCyc:EG10786-MON.

Family and domain databases

InterProIPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
Gene3DG3DSA:3.30.830.10. Pept_M16_core. 1 hit.
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view]
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePTRA_ECOLI
AccessionPrimary (citable) accession number: P05458
Secondary accession number(s): P78106, Q2MA16
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 16, 2009
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents