GBTR_ACIAD
ID GBTR_ACIAD Reviewed; 660 AA.
AC Q6F754;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Glycine betaine transporter {ECO:0000303|PubMed:21567174};
GN OrderedLocusNames=ACIAD3460 {ECO:0000312|EMBL:CAG70111.1};
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, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=21567174; DOI=10.1007/s00203-011-0713-x;
RA Sand M., de Berardinis V., Mingote A., Santos H., Goettig S., Mueller V.,
RA Averhoff B.;
RT "Salt adaptation in Acinetobacter baylyi: identification and
RT characterization of a secondary glycine betaine transporter.";
RL Arch. Microbiol. 193:723-730(2011).
CC -!- FUNCTION: Energy-dependent uptake of glycine betaine in response to
CC high salinity. {ECO:0000269|PubMed:21567174}.
CC -!- ACTIVITY REGULATION: Uptake is activated by NaCl, KCl or mannose
CC gradients across the cell membrane. Inhibited by the protonophore
CC 3,3',4',5-tetrachlorosalicylanilide (TCS).
CC {ECO:0000269|PubMed:21567174}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:21567174}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene completely abolishes glycine
CC betaine transport. {ECO:0000269|PubMed:21567174}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC {ECO:0000305}.
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DR EMBL; CR543861; CAG70111.1; -; Genomic_DNA.
DR RefSeq; WP_004923472.1; NC_005966.1.
DR AlphaFoldDB; Q6F754; -.
DR SMR; Q6F754; -.
DR STRING; 62977.ACIAD3460; -.
DR TCDB; 2.A.15.1.9; the betaine/carnitine/choline transporter (bcct) family.
DR EnsemblBacteria; CAG70111; CAG70111; ACIAD3460.
DR GeneID; 45235645; -.
DR KEGG; aci:ACIAD3460; -.
DR eggNOG; COG1292; Bacteria.
DR HOGENOM; CLU_010118_3_1_6; -.
DR OMA; VHAWAIY; -.
DR OrthoDB; 1217683at2; -.
DR BioCyc; ASP62977:ACIAD_RS15655-MON; -.
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 Stress response; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..660
FT /note="Glycine betaine transporter"
FT /id="PRO_0000435020"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..52
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..139
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..230
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..316
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..401
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..471
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21567174"
SQ SEQUENCE 660 AA; 74117 MW; 9BE862ABEA9FD35E CRC64;
MPSKTSSRFA NINPNVFVST IMIIAIFLAI VILAPDAFEL LTQQLKNWIT ESFSWFYVLS
VAFFLIVLGY IACSSSGKIK LGPDHSQPDY SNSSWFAMLF TAGMGIGLMF FGIAEPIMHY
VSPPSGEPET ILAAQQSMRV TFFHWGLHAW GIYAIVALSL SYFAYRHDLP LKIRSSLYPL
IGKKIYGPMG DAVDTFATIG TIFGVATTLG FGVTQISSGL NYLFGFEPTS FSKVVLIIIV
SAMAALSVGL GLDKGVKRLA ELNLVLAVTL LAFVFFTSAT VYLLQTTIQN TGQYISNLFE
MTFNLYAYQP NGWIGGWTIM YWAWWISWSP FVGMFIARVS RGRTIREFII GVMLIPTGFT
LIWMGFMGNA GLYSILHDGN LSLLNAVQRD SSVALFEFLH SLPFSGVMSL LATVLVVLFF
VTSADSGALV VDYLTAKSED SPVWQRLFWI VVMAGLAIIL LLAGGLTALQ SATIMSALPF
TFIMLLICWG LIKALRIDST KMQAIQEART TPRAIQNPRS WQQRLGLIMH YPHSKVEVDA
YIKKHVQRAF ESLEREFKRR HLTVAISETD DGLQLKVDHH DEINFIYHVV SRETMPPSFM
LEQEHNADVE KYFQAEVFLR EGGQNYDVMD WTEEDLIQDI IDQYERHLYF LSVMRAQTGN
