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Protein

Protease 3

Gene

ptrA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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.PROSITE-ProRule annotation

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi88 – 881ZincPROSITE-ProRule annotation1 Publication
Active sitei91 – 911Proton acceptorPROSITE-ProRule annotation2 Publications
Metal bindingi92 – 921ZincPROSITE-ProRule annotation1 Publication
Metal bindingi169 – 1691Zinc

GO - Molecular functioni

  • metalloendopeptidase activity Source: EcoliWiki
  • metallopeptidase activity Source: EcoCyc
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • protein processing Source: GO_Central
  • proteolysis Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10786-MONOMER.
ECOL316407:JW2789-MONOMER.
MetaCyc:EG10786-MONOMER.

Protein family/group databases

MEROPSiM16.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Protease 3 (EC:3.4.24.55)
Alternative name(s):
Pitrilysin
Protease III
Protease pi
Gene namesi
Name:ptrA
Synonyms:ptr
Ordered Locus Names:b2821, JW2789
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10786. ptrA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi88 – 881H → R: Loss of activity and of Zn-binding.
Mutagenesisi91 – 911E → Q: Loss of activity.
Mutagenesisi92 – 921H → R: Loss of activity and of Zn-binding.
Mutagenesisi162 – 1621E → Q: 20% loss of activity.
Mutagenesisi169 – 1691E → Q: Loss of activity and of Zn-binding.
Mutagenesisi204 – 2041E → Q: No loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 962939Protease 3PRO_0000026758Add
BLAST

Proteomic databases

PaxDbiP05458.
PRIDEiP05458.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4262308. 16 interactions.
IntActiP05458. 11 interactions.
STRINGi511145.b2821.

Structurei

Secondary structure

1
962
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 293Combined sources
Beta strandi43 – 497Combined sources
Beta strandi54 – 596Combined sources
Beta strandi64 – 7310Combined sources
Helixi76 – 783Combined sources
Helixi81 – 833Combined sources
Helixi86 – 938Combined sources
Beta strandi98 – 1014Combined sources
Helixi106 – 1127Combined sources
Turni113 – 1153Combined sources
Beta strandi117 – 1226Combined sources
Beta strandi127 – 1337Combined sources
Helixi135 – 1373Combined sources
Helixi138 – 15013Combined sources
Helixi159 – 17315Combined sources
Helixi177 – 18711Combined sources
Helixi194 – 1963Combined sources
Helixi203 – 2064Combined sources
Helixi214 – 22512Combined sources
Turni228 – 2303Combined sources
Beta strandi232 – 2398Combined sources
Helixi241 – 25010Combined sources
Helixi252 – 2543Combined sources
Helixi272 – 2743Combined sources
Beta strandi275 – 2817Combined sources
Beta strandi289 – 2979Combined sources
Helixi300 – 3056Combined sources
Helixi307 – 31610Combined sources
Helixi323 – 3297Combined sources
Beta strandi333 – 34311Combined sources
Beta strandi346 – 35712Combined sources
Helixi359 – 3635Combined sources
Helixi365 – 38218Combined sources
Helixi386 – 40116Combined sources
Helixi409 – 41911Combined sources
Helixi424 – 4263Combined sources
Turni427 – 4326Combined sources
Helixi439 – 44810Combined sources
Helixi451 – 4533Combined sources
Beta strandi455 – 4595Combined sources
Turni470 – 4723Combined sources
Beta strandi475 – 4806Combined sources
Helixi483 – 49412Combined sources
Beta strandi524 – 5296Combined sources
Beta strandi532 – 5376Combined sources
Beta strandi545 – 55511Combined sources
Helixi557 – 5604Combined sources
Helixi563 – 58927Combined sources
Beta strandi592 – 61221Combined sources
Helixi613 – 62614Combined sources
Helixi632 – 64817Combined sources
Helixi653 – 66311Combined sources
Beta strandi666 – 6683Combined sources
Helixi672 – 6787Combined sources
Helixi679 – 6813Combined sources
Helixi684 – 69512Combined sources
Beta strandi699 – 7079Combined sources
Helixi710 – 72415Combined sources
Beta strandi735 – 7373Combined sources
Beta strandi743 – 7497Combined sources
Beta strandi752 – 7543Combined sources
Beta strandi756 – 7638Combined sources
Helixi769 – 78719Combined sources
Helixi789 – 7924Combined sources
Beta strandi797 – 7993Combined sources
Beta strandi801 – 8088Combined sources
Beta strandi811 – 82313Combined sources
Helixi825 – 84420Combined sources
Helixi848 – 86215Combined sources
Helixi869 – 88214Combined sources
Helixi889 – 89810Combined sources
Helixi902 – 91211Combined sources
Beta strandi917 – 9259Combined sources
Turni930 – 9323Combined sources
Helixi947 – 9515Combined sources
Beta strandi956 – 9583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q2LX-ray2.20A24-962[»]
ProteinModelPortaliP05458.
SMRiP05458. Positions 24-960.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05458.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107QXK. Bacteria.
COG1025. LUCA.
HOGENOMiHOG000124324.
InParanoidiP05458.
KOiK01407.
OMAiGYTQHLP.
OrthoDBiEOG6Z99WW.
PhylomeDBiP05458.

Family and domain databases

Gene3Di3.30.830.10. 4 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
IPR032632. Peptidase_M16_M.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
PF16187. Peptidase_M16_M. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05458-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRSTWFKAL LLLVALWAPL SQAETGWQPI QETIRKSDKD NRQYQAIRLD
60 70 80 90 100
NGMVVLLVSD PQAVKSLSAL VVPVGSLEDP EAYQGLAHYL EHMSLMGSKK
110 120 130 140 150
YPQADSLAEY LKMHGGSHNA STAPYRTAFY LEVENDALPG AVDRLADAIA
160 170 180 190 200
EPLLDKKYAE RERNAVNAEL TMARTRDGMR MAQVSAETIN PAHPGSKFSG
210 220 230 240 250
GNLETLSDKP GNPVQQALKD FHEKYYSANL MKAVIYSNKP LPELAKMAAD
260 270 280 290 300
TFGRVPNKES KKPEITVPVV TDAQKGIIIH YVPALPRKVL RVEFRIDNNS
310 320 330 340 350
AKFRSKTDEL ITYLIGNRSP GTLSDWLQKQ GLVEGISANS DPIVNGNSGV
360 370 380 390 400
LAISASLTDK GLANRDQVVA AIFSYLNLLR EKGIDKQYFD ELANVLDIDF
410 420 430 440 450
RYPSITRDMD YVEWLADTMI RVPVEHTLDA VNIADRYDAK AVKERLAMMT
460 470 480 490 500
PQNARIWYIS PKEPHNKTAY FVDAPYQVDK ISAQTFADWQ KKAADIALSL
510 520 530 540 550
PELNPYIPDD FSLIKSEKKY DHPELIVDES NLRVVYAPSR YFASEPKADV
560 570 580 590 600
SLILRNPKAM DSARNQVMFA LNDYLAGLAL DQLSNQASVG GISFSTNANN
610 620 630 640 650
GLMVNANGYT QRLPQLFQAL LEGYFSYTAT EDQLEQAKSW YNQMMDSAEK
660 670 680 690 700
GKAFEQAIMP AQMLSQVPYF SRDERRKILP SITLKEVLAY RDALKSGARP
710 720 730 740 750
EFMVIGNMTE AQATTLARDV QKQLGADGSE WCRNKDVVVD KKQSVIFEKA
760 770 780 790 800
GNSTDSALAA VFVPTGYDEY TSSAYSSLLG QIVQPWFYNQ LRTEEQLGYA
810 820 830 840 850
VFAFPMSVGR QWGMGFLLQS NDKQPSFLWE RYKAFFPTAE AKLRAMKPDE
860 870 880 890 900
FAQIQQAVIT QMLQAPQTLG EEASKLSKDF DRGNMRFDSR DKIVAQIKLL
910 920 930 940 950
TPQKLADFFH QAVVEPQGMA ILSQISGSQN GKAEYVHPEG WKVWENVSAL
960
QQTMPLMSEK NE
Length:962
Mass (Da):107,708
Last modified:November 1, 1988 - v1
Checksum:i0558C68C2F1A0540
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2848IIIHYVPA → HYHSLRPW in AAA24436 (PubMed:3308636).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF65064. SNECPI.
RefSeqiNP_417298.1. NC_000913.3.
WP_001138201.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75860; AAC75860; b2821.
BAE76890; BAE76890; BAE76890.
GeneIDi947284.
KEGGiecj:JW2789.
eco:b2821.
PATRICi32121060. VBIEscCol129921_2919.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF65064. SNECPI.
RefSeqiNP_417298.1. NC_000913.3.
WP_001138201.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q2LX-ray2.20A24-962[»]
ProteinModelPortaliP05458.
SMRiP05458. Positions 24-960.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262308. 16 interactions.
IntActiP05458. 11 interactions.
STRINGi511145.b2821.

Protein family/group databases

MEROPSiM16.001.

Proteomic databases

PaxDbiP05458.
PRIDEiP05458.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75860; AAC75860; b2821.
BAE76890; BAE76890; BAE76890.
GeneIDi947284.
KEGGiecj:JW2789.
eco:b2821.
PATRICi32121060. VBIEscCol129921_2919.

Organism-specific databases

EchoBASEiEB0779.
EcoGeneiEG10786. ptrA.

Phylogenomic databases

eggNOGiENOG4107QXK. Bacteria.
COG1025. LUCA.
HOGENOMiHOG000124324.
InParanoidiP05458.
KOiK01407.
OMAiGYTQHLP.
OrthoDBiEOG6Z99WW.
PhylomeDBiP05458.

Enzyme and pathway databases

BioCyciEcoCyc:EG10786-MONOMER.
ECOL316407:JW2789-MONOMER.
MetaCyc:EG10786-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP05458.
PROiP05458.

Family and domain databases

Gene3Di3.30.830.10. 4 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
IPR032632. Peptidase_M16_M.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
PF16187. Peptidase_M16_M. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, ACTIVE SITE.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiPTRA_ECOLI
AccessioniPrimary (citable) accession number: P05458
Secondary accession number(s): P78106, Q2MA16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: January 20, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.