TTGC_PSEPT
ID TTGC_PSEPT Reviewed; 484 AA.
AC Q9WWZ8; I7AU11;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Toluene efflux pump outer membrane protein TtgC;
DE Flags: Precursor;
GN Name=ttgC; OrderedLocusNames=T1E_0241;
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 outer membrane component of a constitutive organic
CC solvent efflux system. Is involved in export of toluene, styrene, m-
CC xylene, propylbenzene and ethylbenzene. Also exports AMP and the
CC antibiotics carbenicillin, nalidixic acid, chloramphenicol and
CC tetracycline.
CC -!- SUBCELLULAR LOCATION: Cell outer 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 outer membrane factor (OMF) (TC 1.B.17)
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; AAD39554.1; -; Genomic_DNA.
DR EMBL; CP003734; AFO46100.1; -; Genomic_DNA.
DR RefSeq; WP_003251955.1; NC_018220.1.
DR AlphaFoldDB; Q9WWZ8; -.
DR SMR; Q9WWZ8; -.
DR TCDB; 2.A.6.2.9; the resistance-nodulation-cell division (rnd) superfamily.
DR EnsemblBacteria; AFO46100; AFO46100; T1E_0241.
DR KEGG; ppx:T1E_0241; -.
DR PATRIC; fig|1196325.3.peg.242; -.
DR HOGENOM; CLU_012817_13_3_6; -.
DR Proteomes; UP000006503; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Antibiotic resistance; Cell outer membrane; Lipoprotein; Membrane;
KW Palmitate; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..484
FT /note="Toluene efflux pump outer membrane protein TtgC"
FT /id="PRO_0000031002"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 484 AA; 52848 MW; 4097D58FAF74F958 CRC64;
MTKSLLSLAV TAFILGGCSL IPDYQTPEAP VAAQWPQGPA YSPTQSADVA AAEQGWRQFF
HDPALQQLIQ TSLVNNRDLR VAALNLDAYR AQYRIQRADL FPAVSATGSG SRQRVPANMS
QTGESGITSQ YSATLGVSAY ELDLFGRVRS LTEQALETYL SSEQARRSTQ IALVASVANA
YYTWQADQAL FKLTEETLKT YEESYNLTRR SNEVGVASAL DVSQARTAVE GARVKYSQYQ
RLVAQDVNSL TVLLGTGIPA DLAKPLELDA DQLAEVPAGL PSDILQRRPD IQEAEHLLKA
ANANIGAARA AFFPSISLTA NAGSLSPDMG HLFAGGQGTW LFQPQINLPI FNAGSLKASL
DYSKIQKDIN VAKYEKTIQT AFQEVSDGLA ARKTFEEQLQ AQRDLVQANQ DYYRLAERRY
RIGIDSNLTF LDAQRNLFSA QQALIGDRLS QLTSEVNLYK ALGGGWYEQT GQANQQASVE
TPKG