TCR4_SALOR
ID TCR4_SALOR Reviewed; 394 AA.
AC P33733;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Tetracycline resistance protein, class D;
DE Short=TetA(D);
GN Name=tetA;
OS Salmonella ordonez.
OG Plasmid pIP173.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=612;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BM2000;
RX PubMed=8384294; DOI=10.1007/bf00282811;
RA Allard J.D., Gibson M.L., Vu L.H., Nguyen T.T., Bertrand K.P.;
RT "Nucleotide sequence of class D tetracycline resistance genes from
RT Salmonella ordonez.";
RL Mol. Gen. Genet. 237:301-305(1993).
CC -!- FUNCTION: Resistance to tetracycline by an active tetracycline efflux.
CC This is an energy-dependent process that decreases the accumulation of
CC the antibiotic in whole cells. This protein functions as a metal-
CC tetracycline/H(+) antiporter.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; X65876; CAA46706.1; -; Genomic_DNA.
DR PIR; S30286; S30286.
DR RefSeq; WP_063856073.1; NG_048182.1.
DR AlphaFoldDB; P33733; -.
DR SMR; P33733; -.
DR KEGG; ag:CAA46706; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter 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 Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR01035; TCRTETA.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Antiport; Cell inner membrane; Cell membrane;
KW Hydrogen ion transport; Ion transport; Membrane; Plasmid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..394
FT /note="Tetracycline resistance protein, class D"
FT /id="PRO_0000173395"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 394 AA; 41036 MW; 9DF68F7458928F32 CRC64;
MNKPAVIALV ITLLDAMGIG LIMPVLPSLL REYLPEADVA NHYGILLALY AVMQVCFAPL
LGRWSDKLGR RPVLLLSLAG AAFDYTLLAL SNVLWMLYLG RIISGITGAT GAVAASVVAD
STAVSERTAW FGRLGAAFGA GLIAGPAIGG LAGDISPHLP FVIAAILNAC TFLMVFFIFK
PAVQTEEKPA DEKQESAGIS FITLLKPLAL LLFVFFTAQL IGQIPATVWV LFTESRFAWD
SAAVGFSLAG LGAMHALFQA VVAGALAKRL SEKTIIFAGF IADATAFLLM SAITSGWMVY
PVLILLAGGG IALPALQGII SAGASAANQG KLQGVLVSLT NLTGVAGPLL FAFIFSQTQQ
SADGTVWLIG TALYGLLLAI CLLIRKPAPV AATC
