PET_ECO44
ID PET_ECO44 Reviewed; 1295 AA.
AC O68900; D3H579;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Serine protease pet autotransporter;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Serine protease pet;
DE AltName: Full=Plasmid-encoded toxin pet;
DE Contains:
DE RecName: Full=Serine protease pet translocator;
DE Flags: Precursor;
GN Name=pet; OrderedLocusNames=EC042_pAA035;
OS Escherichia coli O44:H18 (strain 042 / EAEC).
OG Plasmid pAA2.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=216592;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 53-64 AND 1019-1028,
RP AND FUNCTION.
RX PubMed=9632580; DOI=10.1128/iai.66.7.3155-3163.1998;
RA Eslava C., Navarro-Garcia F., Czeczulin J.R., Henderson I.R., Cravioto A.,
RA Nataro J.P.;
RT "Pet, an autotransporter enterotoxin from enteroaggregative Escherichia
RT coli.";
RL Infect. Immun. 66:3155-3163(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=042 / EAEC;
RX PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT "Complete genome sequence and comparative metabolic profiling of the
RT prototypical enteroaggregative Escherichia coli strain 042.";
RL PLoS ONE 5:E8801-E8801(2010).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF SER-260.
RX PubMed=10225873; DOI=10.1128/iai.67.5.2184-2192.1999;
RA Navarro-Garcia F., Sears C., Eslava C., Cravioto A., Nataro J.P.;
RT "Cytoskeletal effects induced by pet, the serine protease enterotoxin of
RT enteroaggregative Escherichia coli.";
RL Infect. Immun. 67:2184-2192(1999).
RN [4]
RP FUNCTION.
RX PubMed=10496914; DOI=10.1128/iai.67.10.5338-5344.1999;
RA Henderson I.R., Hicks S., Navarro-Garcia F., Elias W.P., Philips A.D.,
RA Nataro J.P.;
RT "Involvement of the enteroaggregative Escherichia coli plasmid-encoded
RT toxin in causing human intestinal damage.";
RL Infect. Immun. 67:5338-5344(1999).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF 1018-ASN-ASN-1019.
RX PubMed=11160002; DOI=10.1128/iai.69.2.1053-1060.2001;
RA Navarro-Garcia F., Canizalez-Roman A., Luna J., Sears C., Nataro J.P.;
RT "Plasmid-encoded toxin of enteroaggregative Escherichia coli is
RT internalized by epithelial cells.";
RL Infect. Immun. 69:1053-1060(2001).
CC -!- FUNCTION: Serine protease with enterotoxic and cytotoxic activity.
CC Internalization into the host cell is required for the induction of
CC cytopathic effects. However, the serine activity is not necessary for
CC secretion and internalization into the host cell.
CC {ECO:0000269|PubMed:10225873, ECO:0000269|PubMed:10496914,
CC ECO:0000269|PubMed:11160002, ECO:0000269|PubMed:9632580}.
CC -!- ACTIVITY REGULATION: Inhibition of cytotoxic activity by
CC phenylmethylsulfonyl fluoride. {ECO:0000269|PubMed:10225873}.
CC -!- SUBCELLULAR LOCATION: [Serine protease pet autotransporter]: Periplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Serine protease pet]: Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Serine protease pet translocator]: Cell outer
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Note=The cleaved C-terminal fragment (autotransporter domain) is
CC localized in the outer membrane. {ECO:0000250}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface, with subsequent cleavage.
CC -!- PTM: Cleaved to release the mature protein from the outer membrane.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF056581; AAC26634.1; -; Genomic_DNA.
DR EMBL; FN554767; CBG27789.1; -; Genomic_DNA.
DR RefSeq; WP_014639426.1; NC_017627.1.
DR PDB; 4OM9; X-ray; 2.30 A; A=53-1018.
DR PDBsum; 4OM9; -.
DR AlphaFoldDB; O68900; -.
DR SMR; O68900; -.
DR MEROPS; N04.002; -.
DR MEROPS; S06.004; -.
DR TCDB; 1.B.12.4.4; the autotransporter-1 (at-1) family.
DR KEGG; elo:EC042_pAA035; -.
DR PATRIC; fig|216592.3.peg.5129; -.
DR HOGENOM; CLU_000723_0_0_6; -.
DR OMA; IIGFRVG; -.
DR Proteomes; UP000001407; Plasmid pAA.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR024973; ESPR.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF13018; ESPR; 1.
DR Pfam; PF02395; Peptidase_S6; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Hydrolase;
KW Membrane; Periplasm; Plasmid; Protease; Secreted; Serine protease; Signal;
KW Transmembrane; Transmembrane beta strand; Virulence; Zymogen.
FT SIGNAL 1..52
FT /evidence="ECO:0000269|PubMed:9632580"
FT CHAIN 53..1295
FT /note="Serine protease pet autotransporter"
FT /id="PRO_0000387604"
FT CHAIN 53..1018
FT /note="Serine protease pet"
FT /id="PRO_0000026970"
FT CHAIN 1019..1295
FT /note="Serine protease pet translocator"
FT /id="PRO_0000026971"
FT DOMAIN 54..304
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1029..1295
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT SITE 1018..1019
FT /note="Cleavage"
FT MUTAGEN 260
FT /note="S->I: Loss of protease activity, but does not affect
FT secretion."
FT /evidence="ECO:0000269|PubMed:10225873"
FT MUTAGEN 1018..1019
FT /note="NN->GI: Abolishes secretion."
FT /evidence="ECO:0000269|PubMed:11160002"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:4OM9"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4OM9"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:4OM9"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 224..237
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4OM9"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:4OM9"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 273..287
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:4OM9"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:4OM9"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 413..423
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:4OM9"
FT TURN 469..473
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 513..517
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 531..538
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 554..564
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:4OM9"
FT TURN 589..591
FT /evidence="ECO:0007829|PDB:4OM9"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:4OM9"
FT HELIX 604..610
FT /evidence="ECO:0007829|PDB:4OM9"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 631..647
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 651..661
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 663..666
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:4OM9"
FT TURN 675..678
FT /evidence="ECO:0007829|PDB:4OM9"
FT TURN 683..686
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 692..696
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 707..716
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 720..724
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 734..737
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 749..753
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 755..764
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 769..772
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 777..781
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 785..787
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 792..803
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 818..820
FT /evidence="ECO:0007829|PDB:4OM9"
FT TURN 833..835
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 836..844
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 874..876
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:4OM9"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:4OM9"
SQ SEQUENCE 1295 AA; 139769 MW; 9C6AEF7F345AD429 CRC64;
MNKIYSIKYS AATGGLIAVS ELAKKVICKT NRKISAALLS LAVISYTNII YAANMDISKA
WARDYLDLAQ NKGVFQPGST HVKIKLKDGT DFSFPALPVP DFSSATANGA ATSIGGAYAV
TVAHNAKNKS SANYQTYGST QYTQINRMTT GNDFSIQRLN KYVVETRGAD TSFNYNENNQ
NIIDRYGVDV GNGKKEIIGF RVGSGNTTFS GIKTSQTYQA DLLSASLFHI TNLRANTVGG
NKVEYENDSY FTNLTTNGDS GSGVYVFDNK EDKWVLLGTT HGIIGNGKTQ KTYVTPFDSK
TTNELKQLFI QNVNIDNNTA TIGGGKITIG NTTQDIEKNK NNQNKDLVFS GGGKISLKEN
LDLGYGGFIF DENKKYTVSA EGNNNVTFKG AGIDIGKGST VDWNIKYASN DALHKIGEGS
LNVIQAQNTN LKTGNGTVIL GAQKTFNNIY VAGGPGTVQL NAENALGEGD YAGIFFTENG
GKLDLNGHNQ TFKKIAATDS GTTITNSNTT KESVLSVNNQ NNYIYHGNVD GNVRLEHHLD
TKQDNARLIL DGDIQANSIS IKNAPLVMQG HATDHAIFRT TKTNNCPEFL CGVDWVTRIK
NAENSVNQKN KTTYKSNNQV SDLSQPDWET RKFRFDNLNI EDSSLSIARN ADVEGNIQAK
NSVINIGDKT AYIDLYSGKN ITGAGFTFRQ DIKSGDSIGE SKFTGGIMAT DGSISIGDKA
IVTLNTVSSL DRTALTIHKG ANVTASSSLF TTSNIKSGGD LTLTGATEST GEITPSMFYA
AGGYELTEDG ANFTAKNQAS VTGDIKSEKA AKLSFGSADK DNSATRYSQF ALAMLDGFDT
SYQGSIKAAQ SSLAMNNALW KVTGNSELKK LNSTGSMVLF NGGKNIFNTL TVDELTTSNS
AFVMRTNTQQ ADQLIVKNKL EGANNLLLVD FIEKKGNDKN GLNIDLVKAP ENTSKDVFKT
ETQTIGFSDV TPEIKQQEKD GKSVWTLTGY KTVANADAAK KATSLMSGGY KAFLAEVNNL
NKRMGDLRDI NGEAGAWARI MSGTGSAGGG FSDNYTHVQV GADNKHELDG LDLFTGVTMT
YTDSHAGSDA FSGETKSVGA GLYASAMFES GAYIDLIGKY VHHDNEYTAT FAGLGTRDYS
SHSWYAGAEV GYRYHVTDSA WIEPQAELVY GAVSGKQFSW KDQGMNLTMK DKDFNPLIGR
TGVDVGKSFS GKDWKVTARA GLGYQFDLFA NGETVLRDAS GEKRIKGEKD GRMLMNVGLN
AEIRDNVRFG LEFEKSAFGK YNVDNAINAN FRYSF
