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Protein

Serine protease pet autotransporter

Gene

pet

Organism
Escherichia coli O44:H18 (strain 042 / EAEC)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine protease with enterotoxic and cytotoxic activity. Internalization into the host cell is required for the induction of cytopathic effects. However, the serine activity is not necessary for secretion and internalization into the host cell.4 Publications

Enzyme regulationi

Inhibition of cytotoxic activity by phenylmethylsulfonyl fluoride.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241Charge relay systemPROSITE-ProRule annotation
Active sitei153 – 1531Charge relay systemPROSITE-ProRule annotation
Active sitei260 – 2601Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciECOL216592:GCV7-4989-MONOMER.

Protein family/group databases

MEROPSiS06.004.
TCDBi1.B.12.4.4. the autotransporter-1 (at-1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease pet autotransporter (EC:3.4.21.-)
Cleaved into the following 2 chains:
Alternative name(s):
Plasmid-encoded toxin pet
Gene namesi
Name:pet
Ordered Locus Names:EC042_pAA035
Encoded oniPlasmid pAA20 Publication
OrganismiEscherichia coli O44:H18 (strain 042 / EAEC)
Taxonomic identifieri216592 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001407 Componenti: Plasmid pAA

Subcellular locationi

Serine protease pet translocator :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane, Periplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi260 – 2601S → I: Loss of protease activity, but does not affect secretion. 1 Publication
Mutagenesisi1018 – 10192NN → GI: Abolishes secretion. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 52521 PublicationAdd
BLAST
Chaini53 – 12951243Serine protease pet autotransporterPRO_0000387604Add
BLAST
Chaini53 – 1018966Serine protease petPRO_0000026970Add
BLAST
Chaini1019 – 1295277Serine protease pet translocatorPRO_0000026971Add
BLAST

Post-translational modificationi

Cleaved to release the mature protein from the outer membrane.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1018 – 10192Cleavage

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiO68900.

Structurei

Secondary structure

1
1295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni57 – 593Combined sources
Helixi62 – 698Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi118 – 1225Combined sources
Helixi123 – 1253Combined sources
Beta strandi128 – 13710Combined sources
Beta strandi140 – 14910Combined sources
Beta strandi154 – 1618Combined sources
Helixi179 – 1868Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi224 – 23714Combined sources
Beta strandi240 – 2478Combined sources
Beta strandi249 – 2513Combined sources
Helixi257 – 2593Combined sources
Beta strandi263 – 2686Combined sources
Turni269 – 2724Combined sources
Beta strandi273 – 28715Combined sources
Beta strandi291 – 2966Combined sources
Helixi299 – 3079Combined sources
Beta strandi310 – 3145Combined sources
Beta strandi318 – 3236Combined sources
Beta strandi346 – 3516Combined sources
Beta strandi353 – 3597Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi375 – 3806Combined sources
Helixi381 – 3833Combined sources
Beta strandi387 – 3915Combined sources
Beta strandi393 – 3953Combined sources
Beta strandi400 – 4078Combined sources
Beta strandi413 – 42311Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi435 – 4406Combined sources
Beta strandi449 – 4513Combined sources
Beta strandi456 – 4605Combined sources
Turni469 – 4735Combined sources
Beta strandi474 – 4763Combined sources
Beta strandi481 – 4844Combined sources
Beta strandi490 – 4934Combined sources
Beta strandi503 – 5053Combined sources
Beta strandi509 – 5113Combined sources
Beta strandi513 – 5175Combined sources
Beta strandi523 – 5253Combined sources
Beta strandi527 – 5293Combined sources
Beta strandi531 – 5388Combined sources
Beta strandi548 – 5503Combined sources
Beta strandi554 – 56411Combined sources
Beta strandi566 – 5683Combined sources
Beta strandi580 – 5823Combined sources
Turni589 – 5913Combined sources
Helixi595 – 6028Combined sources
Helixi604 – 6107Combined sources
Helixi613 – 6153Combined sources
Beta strandi616 – 6183Combined sources
Beta strandi631 – 64717Combined sources
Beta strandi651 – 66111Combined sources
Beta strandi663 – 6664Combined sources
Beta strandi669 – 6746Combined sources
Turni675 – 6784Combined sources
Turni683 – 6864Combined sources
Beta strandi692 – 6965Combined sources
Beta strandi701 – 7055Combined sources
Beta strandi707 – 71610Combined sources
Beta strandi720 – 7245Combined sources
Beta strandi728 – 7325Combined sources
Beta strandi734 – 7374Combined sources
Beta strandi742 – 7454Combined sources
Beta strandi749 – 7535Combined sources
Beta strandi755 – 76410Combined sources
Beta strandi769 – 7724Combined sources
Beta strandi777 – 7815Combined sources
Beta strandi785 – 7873Combined sources
Beta strandi792 – 80312Combined sources
Beta strandi805 – 8073Combined sources
Beta strandi818 – 8203Combined sources
Turni833 – 8353Combined sources
Beta strandi836 – 8449Combined sources
Beta strandi846 – 8483Combined sources
Beta strandi874 – 8763Combined sources
Beta strandi893 – 8953Combined sources
Beta strandi967 – 9693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OM9X-ray2.30A53-1018[»]
ProteinModelPortaliO68900.
SMRiO68900. Positions 1019-1295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 304251Peptidase S6PROSITE-ProRule annotationAdd
BLAST
Domaini1029 – 1295267AutotransporterPROSITE-ProRule annotationAdd
BLAST

Domaini

The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent cleavage.

Sequence similaritiesi

Contains 1 autotransporter (TC 1.B.12) domain. [View classification]PROSITE-ProRule annotation
Contains 1 peptidase S6 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

HOGENOMiHOG000117212.
KOiK12684.
OMAiLVMQGHA.

Family and domain databases

Gene3Di2.160.20.20. 1 hit.
2.40.128.130. 1 hit.
InterProiIPR005546. Autotransporte_beta.
IPR024973. ESPR.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR000710. Peptidase_S6.
IPR030396. Peptidase_S6_dom.
[Graphical view]
PfamiPF03797. Autotransporter. 1 hit.
PF13018. ESPR. 1 hit.
PF02395. Peptidase_S6. 1 hit.
[Graphical view]
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF51126. SSF51126. 2 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
PS51691. PEPTIDASE_S6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O68900-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKIYSIKYS AATGGLIAVS ELAKKVICKT NRKISAALLS LAVISYTNII
60 70 80 90 100
YAANMDISKA WARDYLDLAQ NKGVFQPGST HVKIKLKDGT DFSFPALPVP
110 120 130 140 150
DFSSATANGA ATSIGGAYAV TVAHNAKNKS SANYQTYGST QYTQINRMTT
160 170 180 190 200
GNDFSIQRLN KYVVETRGAD TSFNYNENNQ NIIDRYGVDV GNGKKEIIGF
210 220 230 240 250
RVGSGNTTFS GIKTSQTYQA DLLSASLFHI TNLRANTVGG NKVEYENDSY
260 270 280 290 300
FTNLTTNGDS GSGVYVFDNK EDKWVLLGTT HGIIGNGKTQ KTYVTPFDSK
310 320 330 340 350
TTNELKQLFI QNVNIDNNTA TIGGGKITIG NTTQDIEKNK NNQNKDLVFS
360 370 380 390 400
GGGKISLKEN LDLGYGGFIF DENKKYTVSA EGNNNVTFKG AGIDIGKGST
410 420 430 440 450
VDWNIKYASN DALHKIGEGS LNVIQAQNTN LKTGNGTVIL GAQKTFNNIY
460 470 480 490 500
VAGGPGTVQL NAENALGEGD YAGIFFTENG GKLDLNGHNQ TFKKIAATDS
510 520 530 540 550
GTTITNSNTT KESVLSVNNQ NNYIYHGNVD GNVRLEHHLD TKQDNARLIL
560 570 580 590 600
DGDIQANSIS IKNAPLVMQG HATDHAIFRT TKTNNCPEFL CGVDWVTRIK
610 620 630 640 650
NAENSVNQKN KTTYKSNNQV SDLSQPDWET RKFRFDNLNI EDSSLSIARN
660 670 680 690 700
ADVEGNIQAK NSVINIGDKT AYIDLYSGKN ITGAGFTFRQ DIKSGDSIGE
710 720 730 740 750
SKFTGGIMAT DGSISIGDKA IVTLNTVSSL DRTALTIHKG ANVTASSSLF
760 770 780 790 800
TTSNIKSGGD LTLTGATEST GEITPSMFYA AGGYELTEDG ANFTAKNQAS
810 820 830 840 850
VTGDIKSEKA AKLSFGSADK DNSATRYSQF ALAMLDGFDT SYQGSIKAAQ
860 870 880 890 900
SSLAMNNALW KVTGNSELKK LNSTGSMVLF NGGKNIFNTL TVDELTTSNS
910 920 930 940 950
AFVMRTNTQQ ADQLIVKNKL EGANNLLLVD FIEKKGNDKN GLNIDLVKAP
960 970 980 990 1000
ENTSKDVFKT ETQTIGFSDV TPEIKQQEKD GKSVWTLTGY KTVANADAAK
1010 1020 1030 1040 1050
KATSLMSGGY KAFLAEVNNL NKRMGDLRDI NGEAGAWARI MSGTGSAGGG
1060 1070 1080 1090 1100
FSDNYTHVQV GADNKHELDG LDLFTGVTMT YTDSHAGSDA FSGETKSVGA
1110 1120 1130 1140 1150
GLYASAMFES GAYIDLIGKY VHHDNEYTAT FAGLGTRDYS SHSWYAGAEV
1160 1170 1180 1190 1200
GYRYHVTDSA WIEPQAELVY GAVSGKQFSW KDQGMNLTMK DKDFNPLIGR
1210 1220 1230 1240 1250
TGVDVGKSFS GKDWKVTARA GLGYQFDLFA NGETVLRDAS GEKRIKGEKD
1260 1270 1280 1290
GRMLMNVGLN AEIRDNVRFG LEFEKSAFGK YNVDNAINAN FRYSF
Length:1,295
Mass (Da):139,769
Last modified:August 1, 1998 - v1
Checksum:i9C6AEF7F345AD429
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056581 Genomic DNA. Translation: AAC26634.1.
FN554767 Genomic DNA. Translation: CBG27789.1.
RefSeqiWP_014639426.1. NC_017627.1.

Genome annotation databases

KEGGielo:EC042_pAA035.
PATRICi36691751. VBIEscCol52250_5129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056581 Genomic DNA. Translation: AAC26634.1.
FN554767 Genomic DNA. Translation: CBG27789.1.
RefSeqiWP_014639426.1. NC_017627.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OM9X-ray2.30A53-1018[»]
ProteinModelPortaliO68900.
SMRiO68900. Positions 1019-1295.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS06.004.
TCDBi1.B.12.4.4. the autotransporter-1 (at-1) family.

Proteomic databases

PRIDEiO68900.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGielo:EC042_pAA035.
PATRICi36691751. VBIEscCol52250_5129.

Phylogenomic databases

HOGENOMiHOG000117212.
KOiK12684.
OMAiLVMQGHA.

Enzyme and pathway databases

BioCyciECOL216592:GCV7-4989-MONOMER.

Family and domain databases

Gene3Di2.160.20.20. 1 hit.
2.40.128.130. 1 hit.
InterProiIPR005546. Autotransporte_beta.
IPR024973. ESPR.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR000710. Peptidase_S6.
IPR030396. Peptidase_S6_dom.
[Graphical view]
PfamiPF03797. Autotransporter. 1 hit.
PF13018. ESPR. 1 hit.
PF02395. Peptidase_S6. 1 hit.
[Graphical view]
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF51126. SSF51126. 2 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
PS51691. PEPTIDASE_S6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pet, an autotransporter enterotoxin from enteroaggregative Escherichia coli."
    Eslava C., Navarro-Garcia F., Czeczulin J.R., Henderson I.R., Cravioto A., Nataro J.P.
    Infect. Immun. 66:3155-3163(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 53-64 AND 1019-1028, FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 042 / EAEC.
  3. "Cytoskeletal effects induced by pet, the serine protease enterotoxin of enteroaggregative Escherichia coli."
    Navarro-Garcia F., Sears C., Eslava C., Cravioto A., Nataro J.P.
    Infect. Immun. 67:2184-2192(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-260.
  4. "Involvement of the enteroaggregative Escherichia coli plasmid-encoded toxin in causing human intestinal damage."
    Henderson I.R., Hicks S., Navarro-Garcia F., Elias W.P., Philips A.D., Nataro J.P.
    Infect. Immun. 67:5338-5344(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Plasmid-encoded toxin of enteroaggregative Escherichia coli is internalized by epithelial cells."
    Navarro-Garcia F., Canizalez-Roman A., Luna J., Sears C., Nataro J.P.
    Infect. Immun. 69:1053-1060(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 1018-ASN-ASN-1019.

Entry informationi

Entry nameiPET_ECO44
AccessioniPrimary (citable) accession number: O68900
Secondary accession number(s): D3H579
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 96 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, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.