ID BETT2_ACIAD Reviewed; 686 AA.
AC Q6FDF5;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Osmo-dependent choline transporter BetT2 {ECO:0000305};
GN Name=betT2 {ECO:0000303|PubMed:23889709};
GN Synonyms=betT {ECO:0000312|EMBL:CAG67903.1};
GN OrderedLocusNames=ACIAD1012 {ECO:0000312|EMBL:CAG67903.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; 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, SUBCELLULAR 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: Uptake of choline in the presence of high salinity. May
CC primarily serve for osmoprotection. {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-dependent 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; CAG67903.1; -; Genomic_DNA.
DR RefSeq; WP_011182197.1; NC_005966.1.
DR AlphaFoldDB; Q6FDF5; -.
DR SMR; Q6FDF5; -.
DR STRING; 202950.GCA_001485005_01349; -.
DR GeneID; 45233458; -.
DR KEGG; aci:ACIAD1012; -.
DR eggNOG; COG1292; Bacteria.
DR HOGENOM; CLU_010118_3_1_6; -.
DR OrthoDB; 9775735at2; -.
DR BioCyc; ASP62977:ACIAD_RS04665-MONOMER; -.
DR Proteomes; UP000000430; Chromosome.
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 NCBIfam; TIGR00842; bcct; 1.
DR PANTHER; PTHR30047:SF7; HIGH-AFFINITY CHOLINE TRANSPORT PROTEIN; 1.
DR PANTHER; PTHR30047; HIGH-AFFINITY CHOLINE TRANSPORT PROTEIN-RELATED; 1.
DR Pfam; PF02028; BCCT; 1.
DR PROSITE; PS01303; BCCT; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..686
FT /note="Osmo-dependent choline transporter BetT2"
FT /id="PRO_0000435019"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..60
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..150
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..237
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..325
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..412
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..484
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23889709"
SQ SEQUENCE 686 AA; 77562 MW; 07605A8341FD2BE8 CRC64;
MATDNPRAVD DQETHPKDRL NRVVFYVSAL IILIFSLTTI LFNDFANRAL NQVLDWVSST
FSWYYLLAAT LYMVFVIFIA CSRYGNIKLG PKHSKPEFSL LSWSAMLFSA GIGIDLMFFS
VAEPLSHYMH PPVGEGQTYE AARQGMVWTL FHYGLTGWCM YALIGMALGY FSYRYNLPLT
IRSALYPIFG KKINGPIGHS VDTAAVIGTI FGIATTCGIG VVQLNYGLHV LFDLPENLWV
QTALILVAVI ITIISVTSGV NKGLRILSEV NIYVSVGLML FILFLGNTEF LLNALVQNVG
DYLSRFPSLA LESFAFDQPK EWMNSWTLFF WAWWVAWSPF VGLFLARISR GRTIREFVSG
TLIIPLLFTL TWLSIFGNSA LHNVIFDGNI ALAETVLSNP AHGFYDLLAQ YPWFPFIAGV
ATITGLLFYV TSADSGALVL GNFTTQFTNI DHDAPRWLSV FWAVAIGLLT LAMLMTNGIT
ALQNATIIMG LPFSFVMFLV MAGLYKSLRL EDYRQASASL NAAPVVGNVD ILNWKKRLTR
VMHHPGTFET KRMLNEICRP AVHAVAEELQ KRAVQVDVLE VPLEEDEELY HLDITIHLEE
EQNFIYQIWP VRYIAPNFSE RGKRGKQFYY RLETYLYEGS QGNDLVGYTK EQVINDILDR
YERHMTFLHI NRISPGNRPL FPDPKA
//
