ATA_ACIBT
ID ATA_ACIBT Reviewed; 1873 AA.
AC A3M3H0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Adhesin Ata autotransporter;
DE AltName: Full=Acinetobacter trimeric autotransporter;
DE AltName: Full=Type 5 secretion system autotransporter Ata {ECO:0000305};
DE Flags: Precursor;
GN Name=ata; OrderedLocusNames=A1S_1032;
OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS KC755 / 5377).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=400667;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=17344419; DOI=10.1101/gad.1510307;
RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA Gerstein M., Snyder M.;
RT "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT density pyrosequencing and transposon mutagenesis.";
RL Genes Dev. 21:601-614(2007).
RN [2]
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=22825448; DOI=10.1128/iai.06096-11;
RA Bentancor L.V., Routray A., Bozkurt-Guzel C., Camacho-Peiro A., Pier G.B.,
RA Maira-Litran T.;
RT "Evaluation of the trimeric autotransporter Ata as a vaccine candidate
RT against Acinetobacter baumannii infections.";
RL Infect. Immun. 80:3381-3388(2012).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=22609912; DOI=10.1128/jb.06769-11;
RA Bentancor L.V., Camacho-Peiro A., Bozkurt-Guzel C., Pier G.B.,
RA Maira-Litran T.;
RT "Identification of Ata, a multifunctional trimeric autotransporter of
RT Acinetobacter baumannii.";
RL J. Bacteriol. 194:3950-3960(2012).
CC -!- FUNCTION: Important for biofilm formation, binding to various
CC extracellular matrix/basal membrane (ECM/BM) proteins, adhesion to
CC collagen type IV, and for survival in a mouse model of lethal
CC infection. {ECO:0000269|PubMed:22609912}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:22609912}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:22609912}. Cell
CC outer membrane {ECO:0000269|PubMed:22609912}. Note=The C-terminal
CC translocator domain is localized in the outer membrane and the
CC passenger domain is at the cell surface. {ECO:0000269|PubMed:22609912}.
CC -!- INDUCTION: Expression is growth phase dependent. Expressed at high
CC levels during early logarithmic phase, and expression declines
CC throughout the logarithmic and stationary phases.
CC {ECO:0000269|PubMed:22609912}.
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. {ECO:0000269|PubMed:22609912}.
CC -!- DISRUPTION PHENOTYPE: Deletion decreases biofilm formation and
CC decreases the virulence in the murine model of lethal infection.
CC {ECO:0000269|PubMed:22609912}.
CC -!- BIOTECHNOLOGY: Might be a good vaccine candidate. The ability of Ata to
CC engender anti-adhesive, bactericidal, opsonophagocytic, and protective
CC antibodies validates its potential use as an antigenic target against
CC multidrug-resistant A.baumannii infections.
CC {ECO:0000269|PubMed:22825448}.
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; CP000521; ABO11464.2; -; Genomic_DNA.
DR RefSeq; WP_001045587.1; NZ_CP053098.1.
DR AlphaFoldDB; A3M3H0; -.
DR SMR; A3M3H0; -.
DR BindingDB; A3M3H0; -.
DR TCDB; 1.B.40.2.6; the autotransporter-2 (at-2) family.
DR PRIDE; A3M3H0; -.
DR KEGG; acb:A1S_1032; -.
DR HOGENOM; CLU_236391_0_0_6; -.
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; -; 5.
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; 6.
DR Pfam; PF05662; YadA_stalk; 9.
DR SUPFAM; SSF101967; SSF101967; 8.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell outer membrane; Coiled coil; Membrane;
KW Protein transport; Signal; Transmembrane; Transmembrane beta strand;
KW Transport; Virulence.
FT SIGNAL 1..53
FT /evidence="ECO:0000255"
FT CHAIN 54..1873
FT /note="Adhesin Ata autotransporter"
FT /id="PRO_0000429920"
FT TRANSMEM 1818..1828
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 1832..1842
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 1851..1857
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 1861..1872
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT REGION 54..1772
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000305"
FT REGION 606..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1873
FT /note="Translocator domain"
FT /evidence="ECO:0000305"
FT COILED 785..873
FT /evidence="ECO:0000255"
FT COILED 982..1062
FT /evidence="ECO:0000255"
FT COILED 1635..1662
FT /evidence="ECO:0000255"
SQ SEQUENCE 1873 AA; 189661 MW; 7239459CA8AC06E7 CRC64;
MNKVYKVIWN ASIGAWVATS EIAKSKTKTK SKTLNLSAAV LSGVICFAPN AFAGTNTEGG
IGQGTSISGT TSCREGSANT ANQKDIAIGC GAQTQDRTGS NIANRNNPYN NSTGAYAGAM
KQGGAISVGT GAVVEKGLGT AIGSYATTQG ISGVAIGTGA LSSGNTALAV GRQSAATADF
SQAIGNVAAA TGKGSLAIGH SATAEGYRSI AIGSPDIENA DPVAGQAGAA YQPKMATKAT
GKDSIAFGGG AVATEENALA IGAFSESKGK KSVAIGTGAK AQKDNAVVIG DQAEASFEGG
VAIGKGARSE AENSIALGKD SKASQATGES FLTKQSAPTG VLSIGDIGTE RRIQNVADGA
ADSDAATVRQ LKAARTHYVS INDNGQPGGN FENDGATGRN AIAVGVNASA AGREAMAIGG
NAQAIGSGAI AMGSSSQTVG RGDVAIGRNA STQGAEGVNS NQSVAIGDQT KAIGDQSVAI
GADVIAKGNS SVAIGGDDVD KIARDTELSN TYTEITGGTL QAGKYPTTEA NHGSTAVGVQ
AVGTGAFSSA FGMTSKATGD ASSAFGVMSN ASGKGAAAFG AVAQATGDGA SAMGINSLAS
GTNSTAIGSG NKPGEGANAT GNSSAAIGSG AQATGDNSAA IGKGAEATNE NAAAVGGGAK
ATGKNAAAIG GGAIADQENA VAVGQGAQSL VEGGVALGAR SKVEAKNSVA LGQDAVATEA
TGTSFLTNRD ASQSNGVISV GSAGKERRIT NVEDGSADSD AVTVRQLKNV DSRVNQNTSN
IGKNTQNITN LNQKLDDTKT NLGNQIADTN KNLNDAKKDL GNQITDTNTK LNTTKDQLTT
QINDTNTELN NTIGNTKTEL NTKIDNTKTE LENKGLNFAG NSGADVHRKL GDKLNIVGGA
AASTPAAKTS GENVITRTTQ DGIQIELLKD SKFDSVTTGN TTLNTNGLTI KEGPSITKQG
INAGSKQISN VADGINAKDA VNVDQLTKVK DNLNGRITDT NNQLNDAKKD LGNQIADTNK
NLNDAKKDLG NQITDTNTKL NNTKDQLTTQ INDTKTELNN TIGNTKTELN SKIDSTKTEL
ENKGLNFAGN SGADVHRKLG EKLNIIGGAA ASTPAAKTSG ENVITRTTKD GIQIELLKDS
KFDSVTTGNT TLNTNGLTIK EGPSITKDGI NASGKQITNV ADGVNAKDAV NKGQLDNLAA
KQNATDDAAV KYDDAKTKDK VTLKGKDGTV LDNVKAGHIS STSKEAVNGS QIHNISNSIK
NSIGGNTVVN PDGSLTTNNI GGTGKNNIND AISEVKNTAT KAKTTVTEGD NIVVKETVNK
DGSTNYEVST KKDLTLNSVT TGDTVLNNNG LTIKDGPSIT KDGVNAGGKK ITDVANGVIA
QNSKDAVNGA QVHHISNSIK NSIGGNTVVN PDGSLTTNNI GGTGKNNIND AIKSVDEKVT
NGVNDLTQKG LNFGANDQKT TQGKAVHRKL GDTINIVGGA DAKTAEDKTS GENIITRTTE
DGVKIEMLKD VKFDSVNVGG HVLNQQGLII KGGPSITVNG INAGGKQITN VADGINAKDA
VNKGQLDKQI NEVKDQIGKD IGKLSDHAVQ YDKDKNGNVD KSSVTLGGGE KGTNLKNVAD
GKVAEGSKDA VNGGQLWNVQ NQVDKNSNDI KNIQNNIDNI SNGKAGLVQQ QKPNGEITVG
RDTGGTSINM AGKEGDRVVQ GVKDGEIKAG SNQAVNGGQI HKISESIKNS IGGNTTIDPK
DGSITTNNIG GTGKNNINDA IGTLNQSNQE LGNKITNLGD QLQQVFYDTN KRIDDVEKKA
NAGIAAAMAL ENAPFVAGKY TYAVGAAYHG GENAVGVTLR KTSDNGRWSI TGGVAAASQG
EPSVRVGISG VIN
