ID   SADA_SALTY              Reviewed;        1461 AA.
AC   Q8ZL64;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Autotransporter adhesin SadA {ECO:0000305};
DE   AltName: Full=Salmonella adhesin A {ECO:0000303|PubMed:18093992};
DE   AltName: Full=Type 5 secretion system autotransporter SadA {ECO:0000305};
DE   Flags: Precursor;
GN   Name=sadA {ECO:0000303|PubMed:18093992};
GN   OrderedLocusNames=STM3691 {ECO:0000312|EMBL:AAL22550.1};
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=SL1344;
RX   PubMed=21859856; DOI=10.1128/iai.05592-11;
RA   Raghunathan D., Wells T.J., Morris F.C., Shaw R.K., Bobat S., Peters S.E.,
RA   Paterson G.K., Jensen K.T., Leyton D.L., Blair J.M., Browning D.F.,
RA   Pravin J., Flores-Langarica A., Hitchcock J.R., Moraes C.T., Piazza R.M.,
RA   Maskell D.J., Webber M.A., May R.C., MacLennan C.A., Piddock L.J.,
RA   Cunningham A.F., Henderson I.R.;
RT   "SadA, a trimeric autotransporter from Salmonella enterica serovar
RT   Typhimurium, can promote biofilm formation and provides limited protection
RT   against infection.";
RL   Infect. Immun. 79:4342-4352(2011).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24369174; DOI=10.1074/jbc.m113.513275;
RA   Grin I., Hartmann M.D., Sauer G., Hernandez Alvarez B., Schuetz M.,
RA   Wagner S., Madlung J., Macek B., Felipe-Lopez A., Hensel M., Lupas A.,
RA   Linke D.;
RT   "A trimeric lipoprotein assists in trimeric autotransporter biogenesis in
RT   enterobacteria.";
RL   J. Biol. Chem. 289:7388-7398(2014).
RN   [4] {ECO:0007744|PDB:3ZMF}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 304-358.
RX   PubMed=18093992; DOI=10.1093/protein/gzm071;
RA   Hernandez Alvarez B., Hartmann M.D., Albrecht R., Lupas A.N., Zeth K.,
RA   Linke D.;
RT   "A new expression system for protein crystallization using trimeric coiled-
RT   coil adaptors.";
RL   Protein Eng. Des. Sel. 21:11-18(2008).
RN   [5] {ECO:0007744|PDB:2WPQ, ECO:0007744|PDB:2WPR, ECO:0007744|PDB:2WPS}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 479-523.
RX   PubMed=19805097; DOI=10.1073/pnas.0907256106;
RA   Hartmann M.D., Ridderbusch O., Zeth K., Albrecht R., Testa O.,
RA   Woolfson D.N., Sauer G., Dunin-Horkawicz S., Lupas A.N., Alvarez B.H.;
RT   "A coiled-coil motif that sequesters ions to the hydrophobic core.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16950-16955(2009).
RN   [6] {ECO:0007744|PDB:2YNY, ECO:0007744|PDB:2YNZ, ECO:0007744|PDB:2YO0, ECO:0007744|PDB:2YO1, ECO:0007744|PDB:2YO2, ECO:0007744|PDB:2YO3}
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 253-358; 823-947 AND 1049-1386,
RP   AND DOMAIN.
RC   STRAIN=LT2;
RX   PubMed=23213248; DOI=10.1073/pnas.1211872110;
RA   Hartmann M.D., Grin I., Dunin-Horkawicz S., Deiss S., Linke D., Lupas A.N.,
RA   Hernandez Alvarez B.;
RT   "Complete fiber structures of complex trimeric autotransporter adhesins
RT   conserved in enterobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20907-20912(2012).
CC   -!- FUNCTION: Involved in cell aggregation, biofilm formation, and adhesion
CC       to human intestinal epithelial cells. {ECO:0000269|PubMed:21859856}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:21859856}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:21859856}. Cell
CC       outer membrane {ECO:0000269|PubMed:21859856}. Note=The C-terminal
CC       translocator domain is localized in the outer membrane and the
CC       passenger domain is at the cell surface (By similarity). Proper surface
CC       expression requires SadB (PubMed:24369174).
CC       {ECO:0000250|UniProtKB:A0A0H2VCA1, ECO:0000269|PubMed:24369174}.
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 (By similarity). The surface exposed region
CC       contains four YadA-like head domains and extended stalk regions,
CC       multiply segmented by FGG, HANS, DALL and neck motifs
CC       (PubMed:23213248). {ECO:0000250|UniProtKB:A0A0H2VCA1,
CC       ECO:0000269|PubMed:23213248}.
CC   -!- DISRUPTION PHENOTYPE: In vitro, loss of sadA does not affect cell
CC       aggregation, biofilm formation and adhesion to epithelial cells.
CC       Disruption does not affect the course of infection.
CC       {ECO:0000269|PubMed:21859856}.
CC   -!- MISCELLANEOUS: Immunization of mice with folded, full-length, purified
CC       SadA elicits an IgG response which provides limited protection against
CC       bacterial challenge. {ECO:0000269|PubMed:21859856}.
CC   -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC       {ECO:0000305}.
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DR   EMBL; AE006468; AAL22550.1; -; Genomic_DNA.
DR   RefSeq; NP_462591.1; NC_003197.2.
DR   RefSeq; WP_001079584.1; NC_003197.2.
DR   PDB; 2WPQ; X-ray; 1.85 A; A/B/C=479-519.
DR   PDB; 2WPR; X-ray; 2.65 A; A/B/C=483-523.
DR   PDB; 2WPS; X-ray; 2.60 A; A/B/C=483-523.
DR   PDB; 2YNY; X-ray; 1.35 A; A/B/C=253-302.
DR   PDB; 2YNZ; X-ray; 1.40 A; A/B/C=823-947.
DR   PDB; 2YO0; X-ray; 2.80 A; A=1049-1304.
DR   PDB; 2YO1; X-ray; 3.10 A; A/B/C=1061-1304.
DR   PDB; 2YO2; X-ray; 2.00 A; A=253-358.
DR   PDB; 2YO3; X-ray; 2.00 A; A/B/C=1185-1386.
DR   PDB; 3ZMF; X-ray; 1.85 A; A/B/C=304-358.
DR   PDBsum; 2WPQ; -.
DR   PDBsum; 2WPR; -.
DR   PDBsum; 2WPS; -.
DR   PDBsum; 2YNY; -.
DR   PDBsum; 2YNZ; -.
DR   PDBsum; 2YO0; -.
DR   PDBsum; 2YO1; -.
DR   PDBsum; 2YO2; -.
DR   PDBsum; 2YO3; -.
DR   PDBsum; 3ZMF; -.
DR   AlphaFoldDB; Q8ZL64; -.
DR   SMR; Q8ZL64; -.
DR   STRING; 99287.STM3691; -.
DR   PaxDb; 99287-STM3691; -.
DR   GeneID; 1255215; -.
DR   KEGG; stm:STM3691; -.
DR   PATRIC; fig|99287.12.peg.3904; -.
DR   HOGENOM; CLU_002363_1_0_6; -.
DR   OMA; TTQINDT; -.
DR   PhylomeDB; Q8ZL64; -.
DR   BioCyc; SENT99287:STM3691-MONOMER; -.
DR   EvolutionaryTrace; Q8ZL64; -.
DR   Proteomes; UP000001014; 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd12820; LbR_YadA-like; 1.
DR   Gene3D; 1.20.5.170; -; 9.
DR   Gene3D; 1.20.5.2280; -; 1.
DR   Gene3D; 2.60.40.4050; -; 3.
DR   Gene3D; 4.10.80.270; -; 7.
DR   Gene3D; 6.10.250.2040; -; 1.
DR   Gene3D; 3.30.1300.30; GSPII I/J protein-like; 1.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 3.
DR   InterPro; IPR008640; Adhesin_Head_dom.
DR   InterPro; IPR008635; Coiled_stalk_dom.
DR   InterPro; IPR024973; ESPR.
DR   InterPro; IPR045584; Pilin-like.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   InterPro; IPR005594; YadA_C.
DR   Pfam; PF13018; ESPR; 1.
DR   Pfam; PF03895; YadA_anchor; 1.
DR   Pfam; PF05658; YadA_head; 10.
DR   Pfam; PF05662; YadA_stalk; 12.
DR   SUPFAM; SSF101967; Adhesin YadA, collagen-binding domain; 11.
DR   SUPFAM; SSF54523; Pili subunits; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell outer membrane; Membrane; Protein transport;
KW   Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW   Transport.
FT   SIGNAL          1..54
FT                   /evidence="ECO:0000305"
FT   CHAIN           55..1461
FT                   /note="Autotransporter adhesin SadA"
FT                   /id="PRO_0000437739"
FT   TRANSMEM        1407..1417
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT   TRANSMEM        1421..1431
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT   TRANSMEM        1440..1446
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT   TRANSMEM        1450..1461
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT   REGION          55..1372
FT                   /note="Surface exposed passenger domain"
FT                   /evidence="ECO:0000305"
FT   REGION          1373..1461
FT                   /note="Translocator domain"
FT                   /evidence="ECO:0000305"
FT   HELIX           254..265
FT                   /evidence="ECO:0007829|PDB:2YNY"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:2YNY"
FT   STRAND          287..291
FT                   /evidence="ECO:0007829|PDB:2YNY"
FT   HELIX           292..302
FT                   /evidence="ECO:0007829|PDB:2YNY"
FT   STRAND          319..321
FT                   /evidence="ECO:0007829|PDB:2YO2"
FT   TURN            322..324
FT                   /evidence="ECO:0007829|PDB:3ZMF"
FT   STRAND          325..328
FT                   /evidence="ECO:0007829|PDB:3ZMF"
FT   HELIX           478..525
FT                   /evidence="ECO:0007829|PDB:2WPQ"
FT   HELIX           823..849
FT                   /evidence="ECO:0007829|PDB:2YNZ"
FT   STRAND          852..854
FT                   /evidence="ECO:0007829|PDB:2YNZ"
FT   TURN            855..858
FT                   /evidence="ECO:0007829|PDB:2YNZ"
FT   STRAND          859..861
FT                   /evidence="ECO:0007829|PDB:2YNZ"
FT   STRAND          872..875
FT                   /evidence="ECO:0007829|PDB:2YNZ"
FT   HELIX           890..903
FT                   /evidence="ECO:0007829|PDB:2YNZ"
FT   STRAND          1063..1065
FT                   /evidence="ECO:0007829|PDB:2YO1"
FT   STRAND          1081..1083
FT                   /evidence="ECO:0007829|PDB:2YO0"
FT   STRAND          1094..1099
FT                   /evidence="ECO:0007829|PDB:2YO0"
FT   STRAND          1110..1113
FT                   /evidence="ECO:0007829|PDB:2YO0"
FT   STRAND          1120..1122
FT                   /evidence="ECO:0007829|PDB:2YO0"
FT   STRAND          1124..1127
FT                   /evidence="ECO:0007829|PDB:2YO0"
FT   STRAND          1138..1140
FT                   /evidence="ECO:0007829|PDB:2YO0"
FT   STRAND          1155..1157
FT                   /evidence="ECO:0007829|PDB:2YO0"
FT   HELIX           1184..1217
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   HELIX           1219..1225
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   STRAND          1229..1234
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   STRAND          1248..1251
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   STRAND          1262..1265
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   STRAND          1275..1279
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   STRAND          1281..1283
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   STRAND          1285..1290
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   HELIX           1302..1309
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   STRAND          1327..1329
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   STRAND          1333..1335
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   STRAND          1338..1343
FT                   /evidence="ECO:0007829|PDB:2YO3"
FT   HELIX           1355..1387
FT                   /evidence="ECO:0007829|PDB:2YO3"
SQ   SEQUENCE   1461 AA;  147838 MW;  91C59A87E7282254 CRC64;
     MNRIFKVLWN AATGTFVVTS ETAKSRGKKN GRRKLAVSAL IGLSSIMVSA DALANAGNDT
     GDGVTPTGTQ TGGKGWIAIG TDATANTYTN VDGASAAMGY KASAMGKWST AIGSYSQSTG
     DSSLALGVKS VSAGDRAIAM GASSSASGSY SMAMGVYANS SGAKSVALGY KSVASGATSS
     ALGYQATASG DDSAAFGNGA KAIGTNSVAL GSGSVAQEDN SVAVGNSTTQ RQITYVAKGD
     INSTSTDAVT GAQIYSLSQS VADRLGGGAS VNSDGTVNAP LYEVGTGIYN NVGSALSALN
     TSITNTEASV AGLAEDALLW DESISAFSAS HTGNASKITN LAAGTLAADS TDAVNGSQLF
     DTNEKVDKNT ADIATNTGSI NQNTADITAN TDSINQNTTD IAANTTSINQ NTTDIATNTT
     NINSLSDSVT TLTDDALLWD AASGAFSAKH NGSDSKITNL AAGTLAADST DAVNGSQLFD
     TNEKVDQNTA DITTNTNSIN QNTTDIATNT TNINNLSDSI TTLTDDALLW DAASGAFSAN
     HNGSASKITN LAAGTLAADS TDAVNGSQLF ATNENVSQNT ADITTNTNSI NQNTTDIATN
     TTSINNLSDS ITTLTDDALL WDAASGTFSA SRSGSASKIT NLAAGTLAAD STDAVNGSQL
     YETNQKVDQN TSAIADINTS ITNLSSDNLS WNETTSSFSA SHGSSTTNKI TNVAAGELSE
     ESTDAVNGSQ LFETNEKVDQ NTTDIAANTT NITQNSTAIE NLNTSVSDIN TSITGLTDNA
     LLWDEDTGAF SANHGGSTSK ITNVAAGALS EDSTDAVNGS QLYETNQKVD QNTSAIADIN
     TSITNLGTDA LSWDDEEGAF SASHGTSGTN KITNVAAGEI ASDSTDAVNG SQLYETNMLI
     SQYNESISQL AGDTSETYIT ENGTGVKYIR TNDNGLEGQD AYATGNGATA VGYDAVASGA
     GSLALGQNSS SSIEGSIALG SGSTSNRAIT TGIRETSATS DGVVIGYNTT DRELLGALSL
     GTDGESYRQI TNVADGSEAQ DAVTVRQLQN AIGAVTTTPT KYYHANSTEE DSLAVGTDSL
     AMGAKTIVNA DAGIGIGLNT LVMADAINGI AIGSNARANH ANSIAMGNGS QTTRGAQTDY
     TAYNMDTPQN SVGEFSVGSE DGQRQITNVA AGSADTDAVN VGQLKVTDAQ VSRNTQSITN
     LNTQVSNLDT RVTNIENGIG DIVTTGSTKY FKTNTDGADA NAQGADSVAI GSGSIAAAEN
     SVALGTNSVA DEANTVSVGS STQQRRITNV AAGVNNTDAV NVAQLKASEA GSVRYETNAD
     GSVNYSVLNL GDGSGGTTRI GNVSAAVNDT DAVNYAQLKR SVEEANTYTD QKMGEMNSKI
     KGVENKMSGG IASAMAMAGL PQAYAPGANM TSIAGGTFNG ESAVAIGVSM VSESGGWVYK
     LQGTSNSQGD YSAAIGAGFQ W
//