BIOY2_LACLM
ID BIOY2_LACLM Reviewed; 182 AA.
AC A2RI45;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Biotin transporter BioY2;
DE AltName: Full=Biotin ECF transporter S component BioY2;
GN Name=bioY2; OrderedLocusNames=llmg_0332;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [2]
RP SUBUNIT, SUBCELLULAR LOCATION, AND EXPRESSION IN E.COLI.
RC STRAIN=MG1363;
RX PubMed=21135102; DOI=10.1074/jbc.m110.199224;
RA ter Beek J., Duurkens R.H., Erkens G.B., Slotboom D.J.;
RT "Quaternary structure and functional unit of energy coupling factor (ECF)-
RT type transporters.";
RL J. Biol. Chem. 286:5471-5475(2011).
CC -!- FUNCTION: Probably a biotin-binding protein that interacts with the
CC energy-coupling factor (ECF) ABC-transporter complex. Unlike classic
CC ABC transporters this ECF transporter provides the energy necessary to
CC transport a number of different substrates. The substrates themselves
CC are bound by transmembrane, not extracytoplasmic soluble proteins.
CC -!- SUBUNIT: In E.coli forms a stable energy-coupling factor (ECF)
CC transporter complex composed of 2 membrane-embedded substrate-binding
CC protein (S component), 2 ATP-binding proteins (A and A' components) and
CC 2 transmembrane proteins (T component), probably with a stoichiometry
CC of 2:1:1:2. May be able to interact with more than 1 S component at a
CC time. {ECO:0000269|PubMed:21135102}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21135102};
CC Multi-pass membrane protein {ECO:0000305|PubMed:21135102}.
CC -!- SIMILARITY: Belongs to the BioY family. {ECO:0000305}.
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DR EMBL; AM406671; CAL96938.1; -; Genomic_DNA.
DR RefSeq; WP_011834394.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; A2RI45; -.
DR SMR; A2RI45; -.
DR STRING; 416870.llmg_0332; -.
DR EnsemblBacteria; CAL96938; CAL96938; llmg_0332.
DR KEGG; llm:llmg_0332; -.
DR eggNOG; COG1268; Bacteria.
DR HOGENOM; CLU_077931_2_2_9; -.
DR OMA; FWPVPMT; -.
DR PhylomeDB; A2RI45; -.
DR BioCyc; LLAC416870:LLMG_RS01715-MON; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015225; F:biotin transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR003784; BioY.
DR PANTHER; PTHR34295; PTHR34295; 1.
DR Pfam; PF02632; BioY; 1.
DR PIRSF; PIRSF016661; BioY; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..182
FT /note="Biotin transporter BioY2"
FT /id="PRO_0000409005"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 182 AA; 19661 MW; 5484FA5D054FF6A2 CRC64;
MQNTKLYSLT LIALGAAIIA VLSPLAIPIG IVPVTLQTLA VGLVATVLKA RETFFAILLY
LLLGFIGIPV FTGGTSGIAV LFGPTGGFLL AFLVMGTLIS WGLHQIKYKT IPAFIINIVG
HLLMLVIGTL WLKFFTQVDW SLALKLGFTP FVFVEIIKAI LVTIFGLALI RALSHTNKYF
TN