TTGA_PSEPT
ID TTGA_PSEPT Reviewed; 384 AA.
AC Q9WWZ9; I7BPU0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Toluene efflux pump periplasmic linker protein TtgA;
DE Flags: Precursor;
GN Name=ttgA; OrderedLocusNames=T1E_0243;
OS Pseudomonas putida (strain DOT-T1E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1196325;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DOT-T1E;
RX PubMed=9642183; DOI=10.1128/jb.180.13.3323-3329.1998;
RA Ramos J.L., Duque E., Godoy P., Segura A.;
RT "Efflux pumps involved in toluene tolerance in Pseudomonas putida DOT-
RT T1E.";
RL J. Bacteriol. 180:3323-3329(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOT-T1E;
RX PubMed=23815283; DOI=10.1111/1751-7915.12061;
RA Udaondo Z., Molina L., Daniels C., Gomez M.J., Molina-Henares M.A.,
RA Matilla M.A., Roca A., Fernandez M., Duque E., Segura A., Ramos J.L.;
RT "Metabolic potential of the organic-solvent tolerant Pseudomonas putida
RT DOT-T1E deduced from its annotated genome.";
RL Microb. Biotechnol. 6:598-611(2013).
RN [3]
RP EFFLUX PUMP SUBSTRATES.
RC STRAIN=DOT-T1E;
RX PubMed=11395460; DOI=10.1128/jb.183.13.3967-3973.2001;
RA Rojas A., Duque E., Mosqueda G., Golden G., Hurtado A., Ramos J.L.,
RA Segura A.;
RT "Three efflux pumps are required to provide efficient tolerance to toluene
RT in Pseudomonas putida DOT-T1E.";
RL J. Bacteriol. 183:3967-3973(2001).
RN [4]
RP INDUCTION.
RC STRAIN=DOT-T1E;
RX PubMed=14506010; DOI=10.1128/aac.47.10.3067-3072.2003;
RA Teran W., Felipe A., Segura A., Rojas A., Ramos J.L., Gallegos M.T.;
RT "Antibiotic-dependent induction of Pseudomonas putida DOT-T1E TtgABC efflux
RT pump is mediated by the drug binding repressor TtgR.";
RL Antimicrob. Agents Chemother. 47:3067-3072(2003).
CC -!- FUNCTION: The periplasmic linker protein component of a constitutive
CC organic solvent efflux system. Involved in export of toluene, styrene,
CC m-xylene, propylbenzene and ethylbenzene. Also exports AMP and the
CC antibiotics carbenicillin, nalidixic acid, chloramphenicol and
CC tetracycline.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: The ttgABC operon is repressed by toluene; this is mediated
CC by TtgR. The ttgABC operon is induced in response to chloramphenicol
CC and tetracycline. {ECO:0000269|PubMed:14506010}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000305}.
CC -!- CAUTION: There are 4 nearly identical operons in various strains of
CC P.putida. This one and the mepABC operon of strain KT2442-TOL function
CC in solvent and antibiotic efflux; however the arpABC operon of strain
CC S12 functions only in antibiotic efflux. This may be due to different
CC protein expression levels. In strain KT2440 the equivalent operon does
CC not seem to function in toluene efflux. {ECO:0000305}.
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DR EMBL; AF031417; AAD39553.1; -; Genomic_DNA.
DR EMBL; CP003734; AFO46102.1; -; Genomic_DNA.
DR RefSeq; WP_014592249.1; NC_018220.1.
DR AlphaFoldDB; Q9WWZ9; -.
DR SMR; Q9WWZ9; -.
DR TCDB; 2.A.6.2.9; the resistance-nodulation-cell division (rnd) superfamily.
DR EnsemblBacteria; AFO46102; AFO46102; T1E_0243.
DR KEGG; ppx:T1E_0243; -.
DR PATRIC; fig|1196325.3.peg.244; -.
DR HOGENOM; CLU_018816_2_1_6; -.
DR Proteomes; UP000006503; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR043602; CusB_dom_1.
DR InterPro; IPR032317; HlyD_D23.
DR InterPro; IPR006143; RND_pump_MFP.
DR Pfam; PF00529; CusB_dom_1; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR TIGRFAMs; TIGR01730; RND_mfp; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Coiled coil;
KW Lipoprotein; Membrane; Palmitate; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..384
FT /note="Toluene efflux pump periplasmic linker protein TtgA"
FT /id="PRO_0000018718"
FT REGION 362..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..155
FT /evidence="ECO:0000255"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 384 AA; 41249 MW; 1E1F9BE412DCF6C4 CRC64;
MQFKPAVTAL VSAVALATLL SGCKKEEAAP AAQAPQVGVV TIQPQAFTLT SELPGRTSAY
RVAEVRPQVN GIILKRLFKE GSEVKEGQQL YQIDPAVYEA TLANAKANLL ATRSLAERYK
QLIDEQAVSK QEYDDANAKR LQAEASLKSA QIDLRYTKVL APISGRIGRS SFTEGALVSN
GQTDAMATIQ QLDPIYVDVT QSTAELLKLR RDLESGQLQK AGNNAASVQL VLEDGSLFKQ
EGRLEFSEVA VDETTGSVTL RALFPNPDHT LLPGMFVHAR LKAGVNANAI LAPQQGVTRD
LKGAPTALVV NQENKVELRQ LKASRTLGSD WLIEEGLNPG DRLITEGLQY VRPGVEVKVS
DATNVKKPAG PDQANAAKAD AKAE