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 23-FEB-2022, entry version 93. 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; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J01749; AAB59735.1; -; Genomic_DNA. DR PIR; B90923; YTEC32. 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 //