TCR2_ECOLX
ID TCR2_ECOLX Reviewed; 401 AA.
AC P02980;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Tetracycline resistance protein, class B;
DE Short=TetA(B);
DE AltName: Full=Metal-tetracycline/H(+) antiporter;
GN Name=tetA;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn10;
RX PubMed=6319234; DOI=10.1016/0378-1119(83)90170-1;
RA Nguyen T.T., Postle K., Bertrand K.P.;
RT "Sequence homology between the tetracycline-resistance determinants of Tn10
RT and pBR322.";
RL Gene 25:83-92(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn10;
RX PubMed=6298728; DOI=10.1093/nar/11.2.525;
RA Hillen W., Schollmeier K.;
RT "Nucleotide sequence of the Tn10 encoded tetracycline resistance gene.";
RL Nucleic Acids Res. 11:525-539(1983).
RN [3]
RP MUTAGENESIS OF HIS-257.
RC TRANSPOSON=Tn10;
RX PubMed=1848846; DOI=10.1016/s0021-9258(18)38081-5;
RA Yamaguchi A., Adachi K., Akasaka T., Ono N., Sawai T.;
RT "Metal-tetracycline/H+ antiporter of Escherichia coli encoded by a
RT transposon Tn10. Histidine 257 plays an essential role in H+
RT translocation.";
RL J. Biol. Chem. 266:6045-6051(1991).
RN [4]
RP MUTAGENESIS OF LYS-65 AND PHE-66.
RC TRANSPOSON=Tn10;
RX PubMed=2168416; DOI=10.1016/s0021-9258(18)55428-4;
RA Yamaguchi A., Ono N., Akasaka T., Noumi T., Sawai T.;
RT "Metal-tetracycline/H+ antiporter of Escherichia coli encoded by a
RT transposon, Tn10. The role of the conserved dipeptide, Ser65-Asp66, in
RT tetracycline transport.";
RL J. Biol. Chem. 265:15525-15530(1990).
RN [5]
RP TOPOLOGY.
RC TRANSPOSON=Tn10;
RX PubMed=8995300; DOI=10.1074/jbc.272.1.580;
RA Kimura T., Ohnuma M., Sawai T., Yamaguchi A.;
RT "Membrane topology of the transposon 10-encoded metal-tetracycline/H+
RT antiporter as studied by site-directed chemical labeling.";
RL J. Biol. Chem. 272:580-585(1997).
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; V00611; CAA23880.1; -; Genomic_DNA.
DR EMBL; J01830; AAB59094.1; -; Genomic_DNA.
DR PIR; A91505; YTECT0.
DR RefSeq; WP_001089072.1; NZ_WSIP01000050.1.
DR RefSeq; WP_031942563.1; NC_025021.1.
DR RefSeq; YP_001096450.1; NC_009133.1.
DR RefSeq; YP_009060383.1; NC_024960.1.
DR RefSeq; YP_009062970.1; NC_025021.1.
DR AlphaFoldDB; P02980; -.
DR SMR; P02980; -.
DR DIP; DIP-16933N; -.
DR ChEMBL; CHEMBL5821; -.
DR DrugCentral; P02980; -.
DR TCDB; 2.A.1.2.68; the major facilitator superfamily (mfs).
DR GeneID; 59693417; -.
DR GeneID; 66257065; -.
DR OMA; ACFSVAF; -.
DR PRO; PR:P02980; -.
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: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 1: Evidence at protein level;
KW Antibiotic resistance; Antiport; Cell inner membrane; Cell membrane;
KW Membrane; Transmembrane; Transmembrane helix; Transport;
KW Transposable element.
FT CHAIN 1..401
FT /note="Tetracycline resistance protein, class B"
FT /id="PRO_0000173393"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 31..42
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 62..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 92..98
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 120..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 153..158
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 179..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 233..243
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 266..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 296..298
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 299..322
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 323..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 333..356
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 357..365
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT TRANSMEM 366..387
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 388..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8995300"
FT MUTAGEN 65
FT /note="S->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:2168416"
FT MUTAGEN 65
FT /note="S->C: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:2168416"
FT MUTAGEN 66
FT /note="D->E: Moderate resistance to tetracycline."
FT /evidence="ECO:0000269|PubMed:2168416"
FT MUTAGEN 66
FT /note="D->N: Unable to extrude tetracycline."
FT /evidence="ECO:0000269|PubMed:2168416"
FT MUTAGEN 257
FT /note="H->D: No H(+) translocation."
FT /evidence="ECO:0000269|PubMed:1848846"
FT MUTAGEN 257
FT /note="H->E: No H(+) translocation."
FT /evidence="ECO:0000269|PubMed:1848846"
FT CONFLICT 281
FT /note="G -> E (in Ref. 2; CAA23880/AAB59094)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="V -> D (in Ref. 2; CAA23880/AAB59094)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="Q -> E (in Ref. 2; CAA23880/AAB59094)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="A -> T (in Ref. 2; CAA23880/AAB59094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 43267 MW; 3995FBE6297F22EF CRC64;
MNSSTKIALV ITLLDAMGIG LIMPVLPTLL REFIASEDIA NHFGVLLALY ALMQVIFAPW
LGKMSDRFGR RPVLLLSLIG ASLDYLLLAF SSALWMLYLG RLLSGITGAT GAVAASVIAD
TTSASQRVKW FGWLGASFGL GLIAGPIIGG FAGEISPHSP FFIAALLNIV TFLVVMFWFR
ETKNTRDNTD TEVGVETQSN SVYITLFKTM PILLIIYFSA QLIGQIPATV WVLFTENRFG
WNSMMVGFSL AGLGLLHSVF QAFVAGRIAT KWGEKTAVLL GFIADSSAFA FLAFISEGWL
VFPVLILLAG GGIALPALQG VMSIQTKSHQ QGALQGLLVS LTNATGVIGP LLFAVIYNHS
LPIWDGWIWI IGLAFYCIII LLSMTFMLTP QAQGSKQETS A
