ID   SAT_ECOL6               Reviewed;        1295 AA.
AC   Q8FDW4; Q6KD43; Q9F6T1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Serine protease sat autotransporter;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Serine protease sat;
DE     AltName: Full=Secreted autotransporter toxin sat;
DE   Contains:
DE     RecName: Full=Serine protease sat translocator;
DE   Flags: Precursor;
GN   Name=sat; OrderedLocusNames=c3619;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACTIVITY REGULATION, PROTEIN SEQUENCE OF
RP   50-68, AND FUNCTION.
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=11029690; DOI=10.1046/j.1365-2958.2000.02110.x;
RA   Guyer D.M., Henderson I.R., Nataro J.P., Mobley H.L.T.;
RT   "Identification of sat, an autotransporter toxin produced by uropathogenic
RT   Escherichia coli.";
RL   Mol. Microbiol. 38:53-66(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O6:K5:H1 / Nissle 1917;
RX   PubMed=15292145; DOI=10.1128/jb.186.16.5432-5441.2004;
RA   Grozdanov L., Raasch C., Schulze J., Sonnenborn U., Gottschalk G.,
RA   Hacker J., Dobrindt U.;
RT   "Analysis of the genome structure of the nonpathogenic probiotic
RT   Escherichia coli strain Nissle 1917.";
RL   J. Bacteriol. 186:5432-5441(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN   [4]
RP   FUNCTION.
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12117966; DOI=10.1128/iai.70.8.4539-4546.2002;
RA   Guyer D.M., Radulovic S., Jones F.-E., Mobley H.L.T.;
RT   "Sat, the secreted autotransporter toxin of uropathogenic Escherichia coli,
RT   is a vacuolating cytotoxin for bladder and kidney epithelial cells.";
RL   Infect. Immun. 70:4539-4546(2002).
CC   -!- FUNCTION: Shows serine protease activity and displays cytophatic
CC       activity, including elongation, rounding, and detachment of a
CC       proportion of the cells from monolayer in culture. Triggers vacuolation
CC       within the cytoplasm of the human bladder and kidney cells.
CC       {ECO:0000269|PubMed:11029690, ECO:0000269|PubMed:12117966}.
CC   -!- ACTIVITY REGULATION: Inhibited by phenylmethylsulfonyl fluoride and
CC       Pefabloc. {ECO:0000269|PubMed:11029690}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease sat autotransporter]: Periplasm
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease sat]: Secreted. Cell surface.
CC   -!- SUBCELLULAR LOCATION: [Serine protease sat 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Cleaved to release the mature protein from the outer membrane.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN82067.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF289092; AAG30168.1; -; Genomic_DNA.
DR   EMBL; AJ586888; CAE55775.1; -; Genomic_DNA.
DR   EMBL; AE014075; AAN82067.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8FDW4; -.
DR   SMR; Q8FDW4; -.
DR   STRING; 199310.c3619; -.
DR   MEROPS; N04.002; -.
DR   TCDB; 1.B.12.4.6; the autotransporter-1 (at-1) family.
DR   EnsemblBacteria; AAN82067; AAN82067; c3619.
DR   KEGG; ecc:c3619; -.
DR   eggNOG; COG3468; Bacteria.
DR   HOGENOM; CLU_000723_0_0_6; -.
DR   OMA; IIGFRVG; -.
DR   PHI-base; PHI:5262; -.
DR   Proteomes; UP000001410; Chromosome.
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   Cell outer membrane; Direct protein sequencing; Hydrolase; Membrane;
KW   Periplasm; Protease; Secreted; Serine protease; Signal; Transmembrane;
KW   Transmembrane beta strand; Virulence; Zymogen.
FT   SIGNAL          1..49
FT                   /evidence="ECO:0000269|PubMed:11029690"
FT   CHAIN           50..1295
FT                   /note="Serine protease sat autotransporter"
FT                   /id="PRO_0000387608"
FT   CHAIN           50..1018
FT                   /note="Serine protease sat"
FT                   /id="PRO_0000026978"
FT   CHAIN           1019..1295
FT                   /note="Serine protease sat translocator"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026979"
FT   DOMAIN          51..300
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        121
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT   ACT_SITE        256
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT   SITE            1018..1019
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   VARIANT         140
FT                   /note="R -> K (in strain: Nissle 1917)"
FT   VARIANT         352
FT                   /note="D -> N (in strain: Nissle 1917)"
FT   VARIANT         579
FT                   /note="S -> T (in strain: Nissle 1917)"
FT   VARIANT         612
FT                   /note="Y -> H (in strain: Nissle 1917)"
FT   VARIANT         669
FT                   /note="V -> A (in strain: Nissle 1917)"
FT   VARIANT         729
FT                   /note="D -> N (in strain: Nissle 1917)"
FT   VARIANT         894
FT                   /note="N -> D (in strain: Nissle 1917)"
FT   VARIANT         1041
FT                   /note="I -> M (in strain: Nissle 1917)"
FT   CONFLICT        58
FT                   /note="W -> Y (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="R -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1295 AA;  140043 MW;  81122C69273B8FE5 CRC64;
     MNKIYSLKYS AATGGLIAVS ELAKRVSGKT NRKLVATMLS LAVAGTVNAA NIDISNVWAR
     DYLDLAQNKG IFQPGATDVT ITLKNGDKFS FHNLSIPDFS GAAASGAATA IGGSYSVTVA
     HNKKNPQAAE TQVYAQSSYR VVDRRNSNDF EIQRLNKFVV ETVGATPAET NPTTYSDALE
     RYGIVTSDGS KKIIGFRAGS GGTSFINGES KISTNSAYSH DLLSASLFEV TQWDSYGMMI
     YKNDKTFRNL EIFGDSGSGA YLYDNKLEKW VLVGTTHGIA SVNGDQLTWI TKYNDKLVSE
     LKDTYSHKIN LNGNNVTIKN TDITLHQNNA DTTGTQEKIT KDKDIVFTNG GDVLFKDNLD
     FGSGGIIFDE GHEYNINGQG FTFKGAGIDI GKESIVNWNA LYSSDDVLHK IGPGTLNVQK
     KQGANIKIGE GNVILNEEGT FNNIYLASGN GKVILNKDNS LGNDQYAGIF FTKRGGTLDL
     NGHNQTFTRI AATDDGTTIT NSDTTKEAVL AINNEDSYIY HGNINGNIKL THNINSQDKK
     TNAKLILDGS VNTKNDVEVS NASLTMQGHA TEHAIFRSSA NHCSLVFLCG TDWVTVLKET
     ESSYNKKFNS DYKSNNQQTS FDQPDWKTGV FKFDTLHLNN ADFSISRNAN VEGNISANKS
     AITIGDKNVY IDNLAGKNIT NNGFDFKQTI STNLSIGETK FTGGITAHNS QIAIGDQAVV
     TLNGATFLDN TPISIDKGAK VIAQNSMFTT KGIDISGELT MMGIPEQNSK TVTPGLHYAA
     DGFRLSGGNA NFIARNMASV TGNIYADDAA TITLGQPETE TPTISSAYQA WAETLLYGFD
     TAYRGAITAP KATVSMNNAI WHLNSQSSIN RLETKDSMVR FTGDNGKFTT LTVNNLTIDD
     SAFVLRANLA QADQLVVNKS LSGKNNLLLV DFIEKNGNSN GLNIDLVSAP KGTAVDVFKA
     TTRSIGFSDV TPVIEQKNDT DKATWTLIGY KSVANADAAK KATLLMSGGY KAFLAEVNNL
     NKRMGDLRDI NGESGAWARI ISGTGSAGGG FSDNYTHVQV GADNKHELDG LDLFTGVTMT
     YTDSHAGSDA FSGETKSVGA GLYASAMFES GAYIDLIGKY VHHDNEYTAT FAGLGTRDYS
     SHSWYAGAEV GYRYHVTDSA WIEPQAELVY GAVSGKQFSW KDQGMNLTMK DKDFNPLIGR
     TGVDVGKSFS GKDWKVTARA GLGYQFDLFA NGETVLRDAS GEKRIKGEKD GRMLMNVGLN
     AEIRDNLRFG LEFEKSAFGK YNVDNAINAN FRYSF