Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi88ZincPROSITE-ProRule annotation1 Publication1
Active sitei91Proton acceptorPROSITE-ProRule annotation2 Publications1
Metal bindingi92ZincPROSITE-ProRule annotation1 Publication1
Metal bindingi169Zinc1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi88H → R: Loss of activity and of Zn-binding. 1
Mutagenesisi91E → Q: Loss of activity. 1
Mutagenesisi92H → R: Loss of activity and of Zn-binding. 1
Mutagenesisi162E → Q: 20% loss of activity. 1
Mutagenesisi169E → Q: Loss of activity and of Zn-binding. 1
Mutagenesisi204E → Q: No loss of activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
ChainiPRO_000002675824 – 962Protease 3Add BLAST939

Proteomic databases

PaxDbiP05458.
PRIDEiP05458.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4262308. 16 interactors.
IntActiP05458. 11 interactors.
STRINGi511145.b2821.

Structurei

Secondary structure

1962
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 29Combined sources3
Beta strandi43 – 49Combined sources7
Beta strandi54 – 59Combined sources6
Beta strandi64 – 73Combined sources10
Helixi76 – 78Combined sources3
Helixi81 – 83Combined sources3
Helixi86 – 93Combined sources8
Beta strandi98 – 101Combined sources4
Helixi106 – 112Combined sources7
Turni113 – 115Combined sources3
Beta strandi117 – 122Combined sources6
Beta strandi127 – 133Combined sources7
Helixi135 – 137Combined sources3
Helixi138 – 150Combined sources13
Helixi159 – 173Combined sources15
Helixi177 – 187Combined sources11
Helixi194 – 196Combined sources3
Helixi203 – 206Combined sources4
Helixi214 – 225Combined sources12
Turni228 – 230Combined sources3
Beta strandi232 – 239Combined sources8
Helixi241 – 250Combined sources10
Helixi252 – 254Combined sources3
Helixi272 – 274Combined sources3
Beta strandi275 – 281Combined sources7
Beta strandi289 – 297Combined sources9
Helixi300 – 305Combined sources6
Helixi307 – 316Combined sources10
Helixi323 – 329Combined sources7
Beta strandi333 – 343Combined sources11
Beta strandi346 – 357Combined sources12
Helixi359 – 363Combined sources5
Helixi365 – 382Combined sources18
Helixi386 – 401Combined sources16
Helixi409 – 419Combined sources11
Helixi424 – 426Combined sources3
Turni427 – 432Combined sources6
Helixi439 – 448Combined sources10
Helixi451 – 453Combined sources3
Beta strandi455 – 459Combined sources5
Turni470 – 472Combined sources3
Beta strandi475 – 480Combined sources6
Helixi483 – 494Combined sources12
Beta strandi524 – 529Combined sources6
Beta strandi532 – 537Combined sources6
Beta strandi545 – 555Combined sources11
Helixi557 – 560Combined sources4
Helixi563 – 589Combined sources27
Beta strandi592 – 612Combined sources21
Helixi613 – 626Combined sources14
Helixi632 – 648Combined sources17
Helixi653 – 663Combined sources11
Beta strandi666 – 668Combined sources3
Helixi672 – 678Combined sources7
Helixi679 – 681Combined sources3
Helixi684 – 695Combined sources12
Beta strandi699 – 707Combined sources9
Helixi710 – 724Combined sources15
Beta strandi735 – 737Combined sources3
Beta strandi743 – 749Combined sources7
Beta strandi752 – 754Combined sources3
Beta strandi756 – 763Combined sources8
Helixi769 – 787Combined sources19
Helixi789 – 792Combined sources4
Beta strandi797 – 799Combined sources3
Beta strandi801 – 808Combined sources8
Beta strandi811 – 823Combined sources13
Helixi825 – 844Combined sources20
Helixi848 – 862Combined sources15
Helixi869 – 882Combined sources14
Helixi889 – 898Combined sources10
Helixi902 – 912Combined sources11
Beta strandi917 – 925Combined sources9
Turni930 – 932Combined sources3
Helixi947 – 951Combined sources5
Beta strandi956 – 958Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q2LX-ray2.20A24-962[»]
ProteinModelPortaliP05458.
SMRiP05458.
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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti277 – 284IIIHYVPA → HYHSLRPW in AAA24436 (PubMed:3308636).Curated8

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q2LX-ray2.20A24-962[»]
ProteinModelPortaliP05458.
SMRiP05458.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262308. 16 interactors.
IntActiP05458. 11 interactors.
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.
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...

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: November 2, 2016
This is version 154 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.