SADA_SALTY
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 03-AUG-2022, entry version 111.
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; Proteobacteria; 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; Q8ZL64; -.
DR EnsemblBacteria; AAL22550; AAL22550; STM3691.
DR GeneID; 1255215; -.
DR KEGG; stm:STM3691; -.
DR PATRIC; fig|99287.12.peg.3904; -.
DR HOGENOM; CLU_002363_1_0_6; -.
DR OMA; VYTTGSE; -.
DR PhylomeDB; Q8ZL64; -.
DR BioCyc; SENT99287:STM3691-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.150.10.10; -; 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; 5.
DR Pfam; PF05662; YadA_stalk; 12.
DR SUPFAM; SSF101967; SSF101967; 11.
DR SUPFAM; SSF54523; SSF54523; 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
