ATAA_ACIS5
ID ATAA_ACIS5 Reviewed; 3630 AA.
AC K7ZP88;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 23-FEB-2022, entry version 36.
DE RecName: Full=Trimeric autotransporter adhesin AtaA {ECO:0000303|PubMed:23155410};
DE Short=TAA AtaA {ECO:0000303|PubMed:26698633};
DE AltName: Full=Type 5 secretion system autotransporter AtaA {ECO:0000303|PubMed:26698633};
DE Flags: Precursor;
GN Name=ataA {ECO:0000303|PubMed:23155410};
OS Acinetobacter sp. (strain Tol 5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=710648;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Tol 5;
RX PubMed=23155410; DOI=10.1371/journal.pone.0048830;
RA Ishikawa M., Nakatani H., Hori K.;
RT "AtaA, a New Member of the Trimeric Autotransporter Adhesins from
RT Acinetobacter sp. Tol 5 Mediating High Adhesiveness to Various Abiotic
RT Surfaces.";
RL PLoS ONE 7:e48830-e48830(2012).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Tol 5;
RX PubMed=17090933; DOI=10.1271/bbb.60236;
RA Ishii S., Unno H., Miyata S., Hori K.;
RT "Effect of cell appendages on the adhesion properties of a highly adhesive
RT bacterium, Acinetobacter sp. Tol 5.";
RL Biosci. Biotechnol. Biochem. 70:2635-2640(2006).
RN [3]
RP BIOTECHNOLOGY.
RC STRAIN=Tol 5;
RX PubMed=23893702; DOI=10.1002/bit.25012;
RA Ishikawa M., Shigemori K., Hori K.;
RT "Application of the adhesive bacterionanofiber AtaA to a novel microbial
RT immobilization method for the production of indigo as a model chemical.";
RL Biotechnol. Bioeng. 111:16-24(2014).
RN [4]
RP INTERACTION WITH TPGA, SUBCELLULAR LOCATION, AND OPERON.
RX PubMed=27074146; DOI=10.1111/mmi.13398;
RA Ishikawa M., Yoshimoto S., Hayashi A., Kanie J., Hori K.;
RT "Discovery of a novel periplasmic protein that forms a complex with a
RT trimeric autotransporter adhesin and peptidoglycan.";
RL Mol. Microbiol. 101:394-410(2016).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP GLY-3487.
RC STRAIN=Tol 5;
RX PubMed=27305955; DOI=10.1038/srep28020;
RA Yoshimoto S., Nakatani H., Iwasaki K., Hori K.;
RT "An Acinetobacter trimeric autotransporter adhesin reaped from cells
RT exhibits its nonspecific stickiness via a highly stable 3D structure.";
RL Sci. Rep. 6:28020-28020(2016).
RN [6]
RP BIOTECHNOLOGY.
RC STRAIN=Tol 5;
RX PubMed=28720107; DOI=10.1186/s12934-017-0740-7;
RA Yoshimoto S., Ohara Y., Nakatani H., Hori K.;
RT "Reversible bacterial immobilization based on the salt-dependent adhesion
RT of the bacterionanofiber protein AtaA.";
RL Microb. Cell Fact. 16:123-123(2017).
RN [7]
RP DOMAIN, AND MUTAGENESIS BY DOMAIN DELETION.
RC STRAIN=Tol 5;
RX PubMed=31653547; DOI=10.1016/j.jbiosc.2019.09.022;
RA Aoki S., Yoshimoto S., Ishikawa M., Linke D., Lupas A., Hori K.;
RT "Native display of a huge homotrimeric protein fiber on the cell surface
RT after precise domain deletion.";
RL J. Biosci. Bioeng. 129:412-417(2020).
RN [8]
RP FUNCTION IN BIOFILM FORMATION.
RC STRAIN=Tol 5;
RX PubMed=31972092; DOI=10.1021/acs.est.9b06577;
RA Furuichi Y., Yoshimoto S., Inaba T., Nomura N., Hori K.;
RT "Process Description of an Unconventional Biofilm Formation by Bacterial
RT Cells Autoagglutinating through Sticky, Long, and Peritrichate
RT Nanofibers.";
RL Environ. Sci. Technol. 54:2520-2529(2020).
RN [9] {ECO:0007744|PDB:3WP8, ECO:0007744|PDB:3WPA, ECO:0007744|PDB:3WPO, ECO:0007744|PDB:3WPP, ECO:0007744|PDB:3WPR, ECO:0007744|PDB:3WQA}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 2905-3168, X-RAY CRYSTALLOGRAPHY
RP (1.79 ANGSTROMS) OF 3170-3561, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP PRO-3061.
RC STRAIN=Tol 5;
RX PubMed=26698633; DOI=10.1074/jbc.m115.701698;
RA Koiwai K., Hartmann M.D., Linke D., Lupas A.N., Hori K.;
RT "Structural Basis for Toughness and Flexibility in the C-terminal Passenger
RT Domain of an Acinetobacter Trimeric Autotransporter Adhesin.";
RL J. Biol. Chem. 291:3705-3724(2016).
CC -!- FUNCTION: Responsible for autoagglutination, and for adhesion to
CC abiotic and biotic surfaces such as polystyrene (PS), type I collagen,
CC polypropylene (PP), polyvinylchloride (PVC), glass and stainless steel
CC (SS). Adhesion is much stronger than that mediated by Yersinia YadA in
CC a comparative assay. Confers autoagglutination and binding to PS, type
CC I collagen, PP, PVC, glass and SS upon expression in Acinetobacter
CC baylyi strain ADP1 (PubMed:23155410). Involved in rapid, irreversible
CC adherence to polyurethane (PubMed:17090933). Forms an unusual biofilm
CC (PubMed:31972092). An extended, surface exposed fiber binds to quartz
CC crystals, PS and glass. It can be removed by washing in distilled water
CC (PubMed:27305955, PubMed:28720107). {ECO:0000269|PubMed:17090933,
CC ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27305955,
CC ECO:0000269|PubMed:28720107, ECO:0000269|PubMed:31972092}.
CC -!- SUBUNIT: Homotrimer (PubMed:26698633) (Probable). Interacts with TpgA
CC (PubMed:27074146). {ECO:0000269|PubMed:26698633,
CC ECO:0000269|PubMed:27074146, ECO:0000305|PubMed:27305955}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:23155410,
CC ECO:0000269|PubMed:27074146, ECO:0000269|PubMed:27305955}. Cell outer
CC membrane {ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27074146};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:A1JUB7}.
CC Note=Localizes to thin, peritrichate nanofibers (200 nm long, 3.5 nm
CC diameter) on the cell surface; an antibody against residues 699-1014
CC only labels the distal tip of these fibers (PubMed:23155410,
CC PubMed:27074146). The C-terminal translocator domain is probably
CC localized in the outer membrane (Probable).
CC {ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27074146,
CC ECO:0000305|PubMed:23155410}.
CC -!- INDUCTION: Part of the ataA-tpgA operon. {ECO:0000269|PubMed:27074146}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, trimerization
CC and insertion of the C-terminal translocator domain in the outer
CC membrane forms a hydrophilic pore for the translocation of the
CC passenger domain to the bacterial cell surface (By similarity). Seems
CC to have 2 tandemly fused passenger domains; a long N-terminal one
CC (residues 59-2904) and a shorter C-terminal one (residues 2905-3561)
CC (Probable). The C-terminal passenger domain is an entwined, elongated
CC trimer about 450 Angstroms in length that is rigid and yet able to bend
CC somewhat. The ability to bind biotic and abiotic substrates lies in the
CC N-terminal passenger domain (PubMed:26698633). The isolated, trimeric,
CC passenger domain (residues 24-3487) forms fibers 225 nm in length, 4 nm
CC in diameter and has a globular structure at both its N-terminus and
CC near its C-terminus. Its secondary structure is resistant to heat up to
CC 80 degrees Celsius, to treatment at pH 2 and 12, as well as incubation
CC in 0.1 M HCl. The intact fibers adhere rapidly to a quartz crystal
CC microbalance system; heat denatured fibers bind less well as their
CC secondary structure decreases (PubMed:27305955). Targeted small domain
CC deletions show the fine ultrastructure of the fiber (PubMed:27305955).
CC {ECO:0000250|UniProtKB:P0C2W0, ECO:0000269|PubMed:26698633,
CC ECO:0000269|PubMed:27305955, ECO:0000305|PubMed:26698633}.
CC -!- DISRUPTION PHENOTYPE: Loss of rapid, irreversible adhesion to
CC polyurethane, loss of both an anchor-like appendage and a peritrichate
CC fibril-type appendage on the cell surface (PubMed:17090933,
CC PubMed:23155410). Cells retain type 1 and Fil fimbriae (defined by FimA
CC and FilA protein respectively) (PubMed:23155410).
CC {ECO:0000269|PubMed:17090933, ECO:0000269|PubMed:23155410}.
CC -!- BIOTECHNOLOGY: Can be used to immobilize bacteria on a solid support;
CC cells can be removed by washing in distilled water, and will reattach
CC as the ionic strength of the medium increases above 10 mM. The attach-
CC detach cycle can be repeated at least 4 times, each time the cells
CC reattach as well as the first time (PubMed:23893702, PubMed:28720107).
CC Expression in the indigo-producing Acinetobacter strain ST-550 leads to
CC cell adherence to a support material and subsequently 5-fold increased
CC levels of indigo production (PubMed:23893702).
CC {ECO:0000269|PubMed:23893702, ECO:0000269|PubMed:28720107}.
CC -!- MISCELLANEOUS: Insertion of a human rhinovirus protease 3C site allows
CC isolation of the intact, folded passenger domain after protease
CC treatment of whole cells. The protease cuts in the tag as indicated
CC GGGLEVLFLQ|GPG. {ECO:0000269|PubMed:27305955}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
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; AB542908; BAM68255.1; -; Genomic_DNA.
DR PDB; 3WP8; X-ray; 1.97 A; A=2905-3168.
DR PDB; 3WPA; X-ray; 1.79 A; A=3170-3561.
DR PDB; 3WPO; X-ray; 2.40 A; A/B/C=3334-3474.
DR PDB; 3WPP; X-ray; 1.95 A; A=3334-3474.
DR PDB; 3WPR; X-ray; 1.90 A; A/B/C=3170-3332.
DR PDB; 3WQA; X-ray; 2.40 A; A/B/C=3334-3474.
DR PDBsum; 3WP8; -.
DR PDBsum; 3WPA; -.
DR PDBsum; 3WPO; -.
DR PDBsum; 3WPP; -.
DR PDBsum; 3WPR; -.
DR PDBsum; 3WQA; -.
DR SMR; K7ZP88; -.
DR KEGG; ag:BAM68255; -.
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:0007155; P:cell adhesion; 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; 3.
DR Pfam; PF05662; YadA_stalk; 9.
DR SUPFAM; SSF101967; SSF101967; 3.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell outer membrane; Membrane;
KW Protein transport; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..3630
FT /note="Trimeric autotransporter adhesin AtaA"
FT /id="PRO_0000450745"
FT TRANSMEM 3575..3585
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 3589..3599
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 3608..3614
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 3618..3629
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT REGION 24..3487
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000269|PubMed:27305955"
FT REGION 108..315
FT /note="N-terminal YadA-like head"
FT /evidence="ECO:0000305|PubMed:26698633"
FT REGION 316..2904
FT /note="N-terminal stalk"
FT /evidence="ECO:0000305|PubMed:26698633"
FT REGION 2905..3169
FT /note="C-terminal YadA-like head"
FT /evidence="ECO:0000305|PubMed:26698633"
FT REGION 3170..3561
FT /note="C-terminal stalk"
FT /evidence="ECO:0000305|PubMed:26698633"
FT REGION 3539..3574
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT REGION 3575..3630
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT MUTAGEN 326..362
FT /note="Missing: Protein expressed on cell surface,
FT autoagglutination and adherence to glass and polystyrene is
FT normal."
FT /evidence="ECO:0000269|PubMed:27305955"
FT MUTAGEN 328..362
FT /note="Missing: Protein is expressed, but not present on
FT the cell surface, loss of autoagglutination and adherence."
FT /evidence="ECO:0000269|PubMed:27305955"
FT MUTAGEN 335..362
FT /note="Missing: Protein expressed on cell surface,
FT decreased autoagglutination, decreased adherence to glass
FT and polystyrene, isolated fiber has slightly altered
FT morphology."
FT /evidence="ECO:0000269|PubMed:27305955"
FT MUTAGEN 3061
FT /note="P->G: Protects recombinant proteins from degradation
FT in vivo."
FT /evidence="ECO:0000269|PubMed:26698633"
FT MUTAGEN 3487
FT /note="G->GGGLEVLFLQGPG: Inserts a protease site, allows
FT isolation of the intact, folded passenger domain. Protein
FT behaves like wild-type."
FT /evidence="ECO:0000269|PubMed:27305955"
FT HELIX 2905..2912
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 2913..2915
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 2921..2923
FT /evidence="ECO:0007829|PDB:3WP8"
FT HELIX 2924..2928
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 2943..2945
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 2947..2950
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 2952..2954
FT /evidence="ECO:0007829|PDB:3WP8"
FT HELIX 2958..2968
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 2983..2987
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 2998..3001
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3014..3017
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3028..3033
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3042..3047
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3056..3061
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3066..3068
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3070..3075
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3080..3082
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3084..3089
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3098..3101
FT /evidence="ECO:0007829|PDB:3WP8"
FT HELIX 3122..3130
FT /evidence="ECO:0007829|PDB:3WP8"
FT STRAND 3138..3140
FT /evidence="ECO:0007829|PDB:3WP8"
FT HELIX 3143..3145
FT /evidence="ECO:0007829|PDB:3WP8"
FT HELIX 3170..3187
FT /evidence="ECO:0007829|PDB:3WPR"
FT STRAND 3211..3213
FT /evidence="ECO:0007829|PDB:3WPR"
FT HELIX 3214..3231
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3235..3238
FT /evidence="ECO:0007829|PDB:3WPR"
FT STRAND 3242..3248
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3254..3260
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3262..3265
FT /evidence="ECO:0007829|PDB:3WPR"
FT STRAND 3267..3271
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3274..3277
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3280..3283
FT /evidence="ECO:0007829|PDB:3WPA"
FT TURN 3284..3287
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3288..3291
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3294..3297
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3302..3304
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3307..3309
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3315..3318
FT /evidence="ECO:0007829|PDB:3WPR"
FT HELIX 3330..3350
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3361..3363
FT /evidence="ECO:0007829|PDB:3WPO"
FT STRAND 3371..3374
FT /evidence="ECO:0007829|PDB:3WPO"
FT HELIX 3391..3417
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3420..3427
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3432..3435
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3441..3444
FT /evidence="ECO:0007829|PDB:3WPO"
FT STRAND 3452..3457
FT /evidence="ECO:0007829|PDB:3WPO"
FT HELIX 3472..3486
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3491..3493
FT /evidence="ECO:0007829|PDB:3WPA"
FT TURN 3494..3497
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3498..3500
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3504..3506
FT /evidence="ECO:0007829|PDB:3WPA"
FT STRAND 3509..3513
FT /evidence="ECO:0007829|PDB:3WPA"
FT HELIX 3514..3544
FT /evidence="ECO:0007829|PDB:3WPA"
FT HELIX 3545..3548
FT /evidence="ECO:0007829|PDB:3WPA"
SQ SEQUENCE 3630 AA; 359309 MW; D18F71FFFB8028B9 CRC64;
MNKIYKVIWN ATLLAWVAVS ELAKGKTKST TSKSKAKSLS SSVIVGGIIL TTPLSLIAAT
VQVGGGTNSG TTATASTNCA DLYNYQNPEN SGSGAAGNYN AGNPSVCSIA IGENAQGGTS
GTGGSPGIAI GGNSKATGGL SVAIGGYAQA TNVGSIALGT AALSSGFNSL AISRQAAATN
NYSIAIGTTS VSKGVGSIAM GHSTNASGDQ SIAIGSSDAV NSATATTTYD GTTNTQASGS
KSIAIGASAK ASTNNSIALG AGSVTSAQSG NSYLTGVGAS ATNGVVSVGT STATRRIQNV
ADGSAASDAV TVAQLDKAYD DTNGRLAAAL GTGSGAAYNA ANNTYTAPTN IGGTGKNTID
DAIKATQRSV VAGSNIVVTP TTASDGSISY SVATSATPTF TSITVNNAPT AGTDATNKTY
VDSKAAASRT EVAAGSNVSG VVKTTGANGQ DVYTVNANGT TASAGSSAVT VTPGTKDANN
VTDYKVDLSA TTKTDIQKGV DAKNAVDTAG LKFKGDTATT SNTKKLGDTV SITGDTNIST
VATTDGVQVK LNPNLDLGAT GSVKTGNTTI NNAGVTADQV TVGGVVINNT SGINAGGKAI
TNVAAPTNNT DAANKKYVDD AGTALTNLGF GLKAQDGTTV NKKLGEAVDI VGSNSNISTK
VNAGKVEVAL SNTLDLGTTG SVTTGSTVIN NAGVTATQVT ANKVTINNAP TAGTDATNKT
YVDSKAAASR TEVAAGSNVS GVVKTTGANG QDIYAVNANG TTASAGSSAV TVTPGTKDAN
NVTDYKVDLS ATTKTDIQKG VDAKNAVDTA GLKFKGDTAT TSNTKKLGDT VSITGDTNIS
TVATTDGVQV KLNPNLDLGA TGSVKTGNTT INNAGVTADQ VTVGGVVINN TSGINAGGKA
ITNVAAPTNN TDAANKKYVD DAGTALTNLG FGLKAQDGTT VNKKLGEAVD IVGSNSNIST
KVNAGKVEVA LSNTLDLGTT GSVTTGSTVI NNAGVTATQV TANKVTVNNA PTAGTDATNK
TYVDSKAAAS RTEVAAGSNV SGVVKTTGAN GQDVYTVNAN GTTASAGSSA VTVTPGTKDA
NNVTDYKVDL SATTKTDIQK GVDAKNAVDT AGLKFKGDTA TTSNTKKLGD TVSITGDTNI
STVATTDGVQ VKLNPNLDLG ATGSVKTGNT TINNAGVTAD QVTVGGVVIN NTSGINAGGK
AITNVAAPTN NTDAANKKYV DDAGTALTNL GFGLKAQDGT TVNKKLGEAV EVVGADSNIT
TKVAGGQVAI ELNKNLNNLT GITVNDGTNG TNGSTVIGKD GISVKDGSGN TIAGVDNTAL
TVKDGSGNTE TSINQAINTL NAAQGETDKF AVKYDKNADG SVNYNNITLA GTTASSTQDA
TTGKITTTGG TSLNNVASAG DYKDVANASK GVNAGDLNNA VVDATNAATS KGFALQAADG
AKVQKNLGEA VEVVGADSNI TTKVAGGQVA IELNKNLNNL TGITVNDGTN GTNGSTVIGK
DGISVKDGSG NTIAGVDNTA LTVKDGSGNT ETSINQAINT LNAAQGETDK FAVKYDKNTD
GSTNYNSITA GNGNGTAATI GTDTAGNSVV TSGGTKISNV ANGVNASDAV NKGQLDSLST
GLTNTGFGLK AADGNTVNKK LGEAVDVVGA DSNITTKVAG GQVAIELNKN LNNLTGITVN
DGTNGTNGST VIGKDGISIK DGSGNTIAGV DNTALTVKDG SGNTETSINQ AINTLNAAQG
ETDKFAVKYD KNADGSANYN NITLAGTTAS STQDATTGKI TTTGGTSLNN VASAGDYKDV
ANASKGVNAG DLNNAVVDAT NAATSKGFAL QAADGAKVQK NLGEAVEVVG ADSNITTKVV
GGQVAIELNK NLNNLTGITV NDGTNGTNGS TVIGKDGISV KDGSGNTIAG VDNTALTVKD
GSGNTETSIN QAINTLNAAQ GETDKFAVKY DKNADGSVNY NNITLAGTTA SSTQDATTGK
ITTTGGTSLN NVASAGDYKD VANASKGVNA GDLNNAVVDA TNAATSKGFA LQAADGAKVQ
KNLGEAVEVV GADSNITTKV AGGQVAIELN KNLNNLTGIT VNDGTNGTNG STVIGKDGIS
VKDGSGNTIA GVDNTALTVK DGSGNTETSI NQAINTLNAA QGETDKFAVK YDKNADGSVN
YNNITLAGTT ASSTQDATTG KITTTGGTSL NNVASAGDYK DVANASKGVN AGDLNNAVVD
ATNAATSKGF ALQAADGAKV QKNLGEAVEV VGADSNITTK VAGGQVAIEL NKNLNNLTGI
TVNDGTNGTN GSTVIGKDGI SVKDGSGNTI AGVDNTALTV KDGSGNTETS INQAINTLNA
AQGETDKFAV KYDKNADGSA NYNNVTLAGT NGTIISNVKA GAVTSTSTDA INGSQLYGVA
NSVKNAIGGS TTIDATTGAI TTTNIGGTGS NTIDGAISSI KDSATKAKTT VSAGDNVVVT
SGTNADGSTN YEVATAKDVN FDKVTVGSVV VDKSSNTIKG LSNTTWNGTA VSGQAATEDQ
LKTVSDAQGE TDKFAVKYDK NADGSANYNS ITAGNGNGTA ATIGTDTAGN SVVTSGGTKI
SNVANGVNAS DAVNKGQLDS LSTGLTNTGF GLKAADGNTV NKKLGEAVDV VGADSNITTK
VAGGQVAIEL NKNLNNLTGI TVNDGTNGTN GSTVIGKDGI SIKDGSGNTI AGVDNTALTV
KDSSGNTETS INQAINTLNA AQGETDKFAV KYDKNADGSV NYNNVTLAGT NGTIIRNVKA
GAVTSTSTDA INGSQLYDIA NSVKNAIGGS TTRDVTTGAI TTTNIGGTGS NTIDGAISSI
KDSATKAKTT ISAGDNVVVT SGTNADGSTN YEVATAKDVN FDKVTVGNVV VDKANDTIQG
LSNKDLNSTD FATKGRAATE EQLKAVITSN ITEVVDGNGN KVNIIDQVVN TKPDNKNQDS
LFLTYDKQGQ ETTDRLTIGQ TVQKMNTDGI KFFHTNADTS KGDLGTTNDS SAGGLNSTAI
GVNAIVANGA DSSVALGHNT KVNGKQSIAI GSGAEALGNQ SISIGTGNKV TGDHSGAIGD
PTIVNGANSY SVGNNNQVLT DDTFVLGNNV TKTIAGSVVL GNGSAATTGA GEAGYALSVA
TNADKAAITK TTSSTGAVAV GDASSGIYRQ ITGVAAGSVD SDAVNVAQLK AVGNQVVTTQ
TTLVNSLGGN AKVNADGTIT GPTYNVAQGN QTNVGDALTA LDNAINTAAT TSKSTVSNGQ
NIVVSKSKNA DGSDNYEVST AKDLTVDSVK AGDTVLNNAG ITIGNNAVVL NNTGLTISGG
PSVTLAGIDA GNKTIQNVAN AVNATDAVNK GQLDSAINNV NNNVNELANN AVKYDDASKD
KITLGGGATG TTITNVKDGT VAQGSKDAVN GGQLWNVQQQ VDQNTTDISN IKNDINNGTV
GLVQQAGKDA PVTVAKDTGG TTVNVAGTDG NRVVTGVKEG AVNATSKDAV NGSQLNTTNQ
AVVNYLGGGA GYDNITGSFT APSYTVGDSK YNNVGGAIDA LNQADQALNS KIDNVSNKLD
NAFRITNNRI DDVEKKANAG IAAAMALESA PYVPGKYTYA AGAAYHGGEN AVGVTLRKTA
DNGRWSITGG VAAASQGDAS VRIGISGVID
