BETT1_ACIAD
ID BETT1_ACIAD Reviewed; 526 AA.
AC Q6FDF6;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Osmo-independent choline transporter BetT1 {ECO:0000305};
GN Name=betT1 {ECO:0000303|PubMed:23889709};
GN OrderedLocusNames=ACIAD1011 {ECO:0000312|EMBL:CAG67902.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [2]
RP FUNCTION AS A TRANSPORTER, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=23889709; DOI=10.1111/1462-2920.12188;
RA Sand M., Stahl J., Waclawska I., Ziegler C., Averhoff B.;
RT "Identification of an osmo-dependent and an osmo-independent choline
RT transporter in Acinetobacter baylyi: implications in osmostress protection
RT and metabolic adaptation.";
RL Environ. Microbiol. 16:1490-1502(2014).
CC -!- FUNCTION: Sodium-independent high-affinity choline uptake system.
CC Uptake is not proton coupled. May play a role in metabolic adaptation
CC to choline-containing environments. {ECO:0000269|PubMed:23889709}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44.26 uM for choline (in the absence of NaCl)
CC {ECO:0000269|PubMed:23889709};
CC KM=49.86 uM for choline (in the presence of 100 mM NaCl)
CC {ECO:0000269|PubMed:23889709};
CC Vmax=6.8 nmol/min/mg enzyme (in the absence of NaCl)
CC {ECO:0000269|PubMed:23889709};
CC Vmax=8.8 nmol/min/mg enzyme (in the presence of 100 mM NaCl)
CC {ECO:0000269|PubMed:23889709};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:23889709}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutant is impaired in osmo-independent choline
CC uptake activity. The betT1/betT2 double mutant is completely impaired
CC in choline transport. {ECO:0000269|PubMed:23889709}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC {ECO:0000305}.
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DR EMBL; CR543861; CAG67902.1; -; Genomic_DNA.
DR RefSeq; WP_004921791.1; NC_005966.1.
DR AlphaFoldDB; Q6FDF6; -.
DR SMR; Q6FDF6; -.
DR STRING; 62977.ACIAD1011; -.
DR EnsemblBacteria; CAG67902; CAG67902; ACIAD1011.
DR GeneID; 45233457; -.
DR KEGG; aci:ACIAD1011; -.
DR eggNOG; COG1292; Bacteria.
DR HOGENOM; CLU_010118_5_2_6; -.
DR OMA; GERWVKG; -.
DR OrthoDB; 1217683at2; -.
DR BioCyc; ASP62977:ACIAD_RS04660-MON; -.
DR SABIO-RK; Q6FDF6; -.
DR Proteomes; UP000000430; Chromosome.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0071705; P:nitrogen compound transport; IEA:InterPro.
DR InterPro; IPR018093; BCCT_CS.
DR InterPro; IPR000060; BCCT_transptr.
DR PANTHER; PTHR30047; PTHR30047; 1.
DR Pfam; PF02028; BCCT; 1.
DR TIGRFAMs; TIGR00842; bcct; 1.
DR PROSITE; PS01303; BCCT; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..526
FT /note="Osmo-independent choline transporter BetT1"
FT /id="PRO_0000435018"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..56
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..148
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..236
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..323
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..417
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..482
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
SQ SEQUENCE 526 AA; 58181 MW; 8C73D8BA2963A29D CRC64;
MWSKRDEQKT YPPIRLNPFV FWSSAISISI FGMLFVLFPE TSQHGLTWIQ QQVNQLFGWY
YMLVIILSLG FVAWLAFSQV GNIPLGKAQD KPEFGYLVWT SMLFSAGIGI ALLYYGVAEP
VDHFLRPPEG QGGTVEAAQN AMMYSFLHWG IHGWVLYALV GVTLGYFAFR RDLPLALRSA
LYPIFGERIH GLVGHMVDGF GILATIISLV TNLGIGALVM ISGISYLFPD LPNTSSTLVV
TVIMMMLVAT LTTVIGIEKG LAWLSRINLR LLYLLLLFVF LTGPTNHLLN GLVQNTGDYL
SHFVQKSFDL YLYDKNATGW LASWTIFYWA WWIAWAPFVG MFIARISKGR TIREVVLGVC
LIPLGFTLAW ISIFGNTAID LILNHGQQII GSLVIQDPAL SLFKLLEYLP FHPYVAGIVV
VICFVLFLTP VGSGTLMIAN LSSQGGSSDS DSPIWLRVFW SIAITIVSIG LLLAGSFSAM
QSAVVLCGLP FSVILLLYMF GLAKALKQET QQPVVESHTT ETSGSD
