TCR3_ECOLX
ID TCR3_ECOLX Reviewed; 396 AA.
AC P02981;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Tetracycline resistance protein, class C;
DE Short=TetA(C);
GN Name=tetA;
OS Escherichia coli.
OG Plasmid pSC101.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=383387; DOI=10.1101/sqb.1979.043.01.013;
RA Sutcliffe J.G.;
RT "Complete nucleotide sequence of the Escherichia coli plasmid pBR322.";
RL Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1979).
RN [2]
RP SEQUENCE REVISION, AND IDENTIFICATION OF PROTEIN.
RX PubMed=6337373; DOI=10.1073/pnas.80.1.237;
RA Livneh Z.;
RT "Directed mutagenesis method for analysis of mutagen specificity:
RT application to ultraviolet-induced mutagenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:237-241(1983).
RN [3]
RP SEQUENCE REVISION, AND IDENTIFICATION OF PROTEIN.
RX PubMed=6307828; DOI=10.1016/0378-1119(83)90112-9;
RA Peden K.W.C.;
RT "Revised sequence of the tetracycline-resistance gene of pBR322.";
RL Gene 22:277-280(1983).
RN [4]
RP TOPOLOGY.
RX PubMed=1517220; DOI=10.1016/s0021-9258(19)37116-9;
RA Allard J.D., Bertrand K.P.;
RT "Membrane topology of the pBR322 tetracycline resistance protein. TetA-PhoA
RT gene fusions and implications for the mechanism of TetA membrane
RT insertion.";
RL J. Biol. Chem. 267:17809-17819(1992).
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 -!- BIOTECHNOLOGY: This protein is used as a marker in many commonly used
CC cloning vectors, such as pBR322 and pACYC184.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; J01749; AAB59735.1; -; Genomic_DNA.
DR PIR; B90923; YTEC32.
DR AlphaFoldDB; P02981; -.
DR SMR; P02981; -.
DR TCDB; 2.A.1.2.102; the major facilitator superfamily (mfs).
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 1: Evidence at protein level;
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..396
FT /note="Tetracycline resistance protein, class C"
FT /id="PRO_0000173394"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 28..45
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 67..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 101..103
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 125..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 160
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 182..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 232..246
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 268..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 299
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 321..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 361..364
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 386..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1517220"
SQ SEQUENCE 396 AA; 41510 MW; 0B9C82E811A2F7DF CRC64;
MKSNNALIVI LGTVTLDAVG IGLVMPVLPG LLRDIVHSDS IASHYGVLLA LYALMQFLCA
PVLGALSDRF GRRPVLLASL LGATIDYAIM ATTPVLWILY AGRIVAGITG ATGAVAGAYI
ADITDGEDRA RHFGLMSACF GVGMVAGPVA GGLLGAISLH APFLAAAVLN GLNLLLGCFL
MQESHKGERR PMPLRAFNPV SSFRWARGMT IVAALMTVFF IMQLVGQVPA ALWVIFGEDR
FRWSATMIGL SLAVFGILHA LAQAFVTGPA TKRFGEKQAI IAGMAADALG YVLLAFATRG
WMAFPIMILL ASGGIGMPAL QAMLSRQVDD DHQGQLQGSL AALTSLTSIT GPLIVTAIYA
ASASTWNGLA WIVGAALYLV CLPALRRGAW SRATST
