TDEA_AGGAC
ID TDEA_AGGAC Reviewed; 457 AA.
AC Q2EHL7;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Toxin and drug export protein A {ECO:0000303|PubMed:17116373};
DE Flags: Precursor;
GN Name=tdeA {ECO:0000303|PubMed:17116373};
OS Aggregatibacter actinomycetemcomitans (Actinobacillus
OS actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=IDH781;
RX PubMed=17116373; DOI=10.1016/j.gene.2006.10.004;
RA Crosby J.A., Kachlany S.C.;
RT "TdeA, a TolC-like protein required for toxin and drug export in
RT Aggregatibacter (Actinobacillus) actinomycetemcomitans.";
RL Gene 388:83-92(2007).
RN [2]
RP SUBUNIT, AND CHARACTERIZATION OF THE PERIPLASMIC DOMAIN.
RX PubMed=18633280;
RA Kim S., Yum S., Jo W.S., Lee B.L., Jeong M.H., Ha N.C.;
RT "Expression and biochemical characterization of the periplasmic domain of
RT bacterial outer membrane porin TdeA.";
RL J. Microbiol. Biotechnol. 18:845-851(2008).
CC -!- FUNCTION: Required for secretion of the LtxA leukotoxin and resistance
CC to various antimicrobial compounds. {ECO:0000269|PubMed:17116373}.
CC -!- SUBUNIT: Homotrimer (PubMed:18633280). Probably part of a complex
CC composed of LtxB, LtxD and TdeA, which forms a single transport channel
CC across the two membranes (PubMed:17116373).
CC {ECO:0000269|PubMed:18633280, ECO:0000303|PubMed:17116373}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:P77211}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P77211}.
CC -!- DOMAIN: The periplasmic domain interacts in vitro with purified
CC peptidoglycans. {ECO:0000269|PubMed:18633280}.
CC -!- DISRUPTION PHENOTYPE: Mutant cannot secrete leukotoxin and is more
CC sensitive to clotrimazole, erythromycin, ethidium bromide, cationic
CC detergents, bile-acids, anionic detergents and chloramphenicol.
CC {ECO:0000269|PubMed:17116373}.
CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC family. {ECO:0000305}.
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DR EMBL; DQ378166; ABD38133.1; -; Genomic_DNA.
DR RefSeq; WP_005545419.1; NZ_VSEW01000002.1.
DR AlphaFoldDB; Q2EHL7; -.
DR SMR; Q2EHL7; -.
DR STRING; 714.ACT75_10870; -.
DR TCDB; 1.B.17.3.11; the outer membrane factor (omf) family.
DR eggNOG; COG1538; Bacteria.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR003423; OMP_efflux.
DR InterPro; IPR010131; RND_efflux_OM_lipoprot_NodT.
DR Pfam; PF02321; OEP; 2.
DR TIGRFAMs; TIGR01845; outer_NodT; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Cell outer membrane; Ion transport; Membrane; Porin;
KW Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..457
FT /note="Toxin and drug export protein A"
FT /id="PRO_0000431390"
SQ SEQUENCE 457 AA; 51118 MW; F4AE6BEB1F8510BA CRC64;
MFTIKKLTLT IVVATTLTGC ANIGDSYRAS LKNYKQYEEI TKQYNIKNDW WKLYKDAQLN
RVVEKALLNN KDLAKATISV NRALYSANLA GANLVPAFSG STRSTAQKNI KTGGNSTISH
TGSLNVSYTL DLWFRLADTA DAAEWAHKAT VQDMESTKLS LINSVVTTYY QIAYLNDAIS
TTKESIKYYT DISNIMRNRL AQGVADSISV DQAQQAVLTA RNNLITYQLN RKTAEQTLRN
LLNLKPDETL KITFPHILKV KSVGVNLNVP VSVIANRPDI KGYQARLSSA FKNVKATEKS
WFPEITLGGS LNSSGKKLNS ATNTLIGGGA LGISLPFLNW NTVKWNVKIS EADYETARLN
YEKSITVALN DVDTNYFSFT QAKKRFTNAQ KTYIYNQRIT QYYRNRYNAG VSELREWLTA
ANTEKNSQLS ILQAKYNVIQ AENAVYSSMA GYYSVKK