ID   TPGA_ACIS5              Reviewed;         264 AA.
AC   A0A160PB22;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Trimeric autotransporter adhesin- and peptidogylcan-associated protein A {ECO:0000303|PubMed:27074146};
DE            Short=TAA- and PGN-associated protein A {ECO:0000303|PubMed:27074146};
DE            Short=TpgA {ECO:0000303|PubMed:27074146};
DE   Flags: Precursor;
GN   Name=tpgA {ECO:0000303|PubMed:27074146};
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], PROTEIN SEQUENCE OF N-TERMINUS,
RP   PEPTIDOGLYCAN-BINDING, INTERACTION WITH ATAA, SUBUNIT, OPERON, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=Tol 5;
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).
CC   -!- FUNCTION: Required for proper surface expression of the autotransporter
CC       adhesin AtaA. Probably assists in the secretion of the passenger domain
CC       of AtaA from the periplasm to the extracellular environment across the
CC       cell outer membrane. Binds peptidoglycan.
CC       {ECO:0000269|PubMed:27074146}.
CC   -!- SUBUNIT: Monomer. Stably interacts with AtaA.
CC       {ECO:0000269|PubMed:27074146}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000269|PubMed:27074146}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:27074146}; Periplasmic side {ECO:0000305}.
CC       Periplasm {ECO:0000269|PubMed:27074146}. Note=Associates with the outer
CC       membrane in wild-type cells, if the ataA gene is deleted it is found in
CC       the periplasm. {ECO:0000269|PubMed:27074146}.
CC   -!- INDUCTION: Part of the ataA-tpgA operon. {ECO:0000269|PubMed:27074146}.
CC   -!- DISRUPTION PHENOTYPE: Decreases adhesiveness of cells to polystyrene.
CC       No change in the amount of AtaA associated with the cell outer
CC       membrane, but greatly reduced amounts of correctly targeted AtaA;
CC       significantly decreased AtaA immunofluorescence and nanofibers on the
CC       cell surface, and greatly increased amounts of AtaA passenger domain in
CC       the periplasm. No visible change in the amount of Omp38 in the outer
CC       membrane. {ECO:0000269|PubMed:27074146}.
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DR   EMBL; LC003235; BAU88430.1; -; Genomic_DNA.
DR   RefSeq; WP_009585404.1; NZ_AP024708.1.
DR   AlphaFoldDB; A0A160PB22; -.
DR   SMR; A0A160PB22; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd07185; OmpA_C-like; 1.
DR   Gene3D; 3.30.1330.60; -; 1.
DR   Gene3D; 3.30.1450.10; -; 1.
DR   InterPro; IPR037873; BamE-like.
DR   InterPro; IPR007450; Lipoprotein_SmpA/OmlA.
DR   InterPro; IPR006664; OMP_bac.
DR   InterPro; IPR006665; OmpA-like.
DR   InterPro; IPR036737; OmpA-like_sf.
DR   Pfam; PF00691; OmpA; 1.
DR   Pfam; PF04355; SmpA_OmlA; 1.
DR   PRINTS; PR01021; OMPADOMAIN.
DR   SUPFAM; SSF103088; SSF103088; 1.
DR   PROSITE; PS51123; OMPA_2; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Direct protein sequencing; Membrane; Periplasm;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:27074146"
FT   CHAIN           24..264
FT                   /note="Trimeric autotransporter adhesin- and peptidogylcan-
FT                   associated protein A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5007818315"
FT   DOMAIN          142..264
FT                   /note="OmpA-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
SQ   SEQUENCE   264 AA;  30250 MW;  18DA734A6A6891E7 CRC64;
     MKAFNKKIMF GVFSGLVMSL SHAAEVESAN TQEIHFPEIK DSYLKQVNRY EYDDVARLDK
     GLTKDQIRHI LGNPQFSEGL FAVKTWNYVL DIREPNSNQY KRCQLRIDFD KQYRSDNLYW
     KGEQCQGLMA WGINNQSETE QTTLAPGGQS ASVLFYFDHA DKNGVKNAEV IRKIADQIKQ
     SDANSPVFVA GYTDRLGSFQ YNQRLSAQRA NTVVELLKQQ GIRGEQIQYS AENKTDVYQK
     CAGINKKIQL VECLAPNRRV NITW