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Database: UniProt
Entry: Q2KBF3_RHIEC
LinkDB: Q2KBF3_RHIEC
Original site: Q2KBF3_RHIEC 
ID   Q2KBF3_RHIEC            Unreviewed;       439 AA.
AC   Q2KBF3;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Tetracycline efflux transporter protein {ECO:0000313|EMBL:ABC89833.1};
GN   Name=tetA {ECO:0000313|EMBL:ABC89833.1};
GN   OrderedLocusNames=RHE_CH01023 {ECO:0000313|EMBL:ABC89833.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC89833.1, ECO:0000313|Proteomes:UP000001936};
RN   [1] {ECO:0000313|EMBL:ABC89833.1, ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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. {ECO:0000256|ARBA:ARBA00003279}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000256|ARBA:ARBA00007520}.
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DR   EMBL; CP000133; ABC89833.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2KBF3; -.
DR   KEGG; ret:RHE_CH01023; -.
DR   eggNOG; COG2814; Bacteria.
DR   HOGENOM; CLU_001265_10_11_5; -.
DR   Proteomes; UP000001936; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd17388; MFS_TetA; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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-like.
DR   PANTHER; PTHR23504; MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 10; 1.
DR   PANTHER; PTHR23504:SF31; MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 10; 1.
DR   Pfam; PF07690; MFS_1; 2.
DR   PRINTS; PR01035; TCRTETA.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        47..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        252..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        376..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          46..433
FT                   /note="Major facilitator superfamily (MFS) profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50850"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  46254 MW;  587F6F05B87B61F4 CRC64;
     MRFSHGSAST SLKPTPDQIR PHREPSAHSV GARALASTRN APMTRSLIVI FTAIVLDAVG
     IGLIFPILPS LLQEITHAQN VAPTIGAMTA LYALMQFIFA PVLGALSDRL GRRPVLLISL
     AGAAVNYLFL AFAPNLTLLF VGRAIAGLTS ANISVATAYI TDISPEEKRA RRFGLFNAMF
     GLGFIIGPVA GGVLGDHWLR LPFIAAAVLN GANLLLAVFI LPESRPGSRE TIDLAALNPL
     KPLRSVLEVK SLLPIVILFF IFSATGEAYG TCWALWGSDA FHWNGLSIGL SLGAFGICQT
     LAQALLPGPA VRLLGERAAI LVGVAGVSLA LTVMAFAGQG WMIFAVMPIF TLGGIGVPAL
     QSLATRQVDE NSQGQFQGVL ASVVSLASIA APLGFSSLYF LVREEWPGAI WLSVVAVYAL
     TVPLVLGLRL KTAERAAVS
//
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