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 07-SEP-2016, entry version 83. 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; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=383387; RA Sutcliffe J.G.; RT "Complete nucleotide sequence of the Escherichia coli plasmid RT 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. RT TetA-PhoA gene fusions and implications for the mechanism of TetA RT membrane insertion."; RL J. Biol. Chem. 267:17809-17819(1992). CC -!- FUNCTION: Resistance to tetracycline by an active tetracycline CC efflux. This is an energy-dependent process that decreases the CC accumulation of the antibiotic in whole cells. This protein CC functions as a metal-tetracycline/H(+) antiporter. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein. CC -!- BIOTECHNOLOGY: This protein is used as a marker in many commonly CC used 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 ProteinModelPortal; P02981; -. DR BioCyc; RETL1328306-WGS:GSTH-1048-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-2999-MONOMER; -. 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:0015992; P:proton transport; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR CDD; cd06174; MFS; 1. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. 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; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 396 Tetracycline resistance protein, class C. FT /FTId=PRO_0000173394. FT TOPO_DOM 1 6 Cytoplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 7 27 Helical. {ECO:0000305}. FT TOPO_DOM 28 45 Periplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 46 66 Helical. {ECO:0000305}. FT TOPO_DOM 67 79 Cytoplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 80 100 Helical. {ECO:0000305}. FT TOPO_DOM 101 103 Periplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 104 124 Helical. {ECO:0000305}. FT TOPO_DOM 125 138 Cytoplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 139 159 Helical. {ECO:0000305}. FT TOPO_DOM 160 160 Periplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 161 181 Helical. {ECO:0000305}. FT TOPO_DOM 182 210 Cytoplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 211 231 Helical. {ECO:0000305}. FT TOPO_DOM 232 246 Periplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 247 267 Helical. {ECO:0000305}. FT TOPO_DOM 268 277 Cytoplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 278 298 Helical. {ECO:0000305}. FT TOPO_DOM 299 299 Periplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 300 320 Helical. {ECO:0000305}. FT TOPO_DOM 321 339 Cytoplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 340 360 Helical. {ECO:0000305}. FT TOPO_DOM 361 364 Periplasmic. FT {ECO:0000305|PubMed:1517220}. FT TRANSMEM 365 385 Helical. {ECO:0000305}. FT TOPO_DOM 386 396 Cytoplasmic. FT {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 //