ID   BIOY_LACLM              Reviewed;         189 AA.
AC   A2RMJ9;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Biotin transporter BioY;
DE   AltName: Full=Biotin ECF transporter S component BioY;
GN   Name=bioY; OrderedLocusNames=llmg_1964;
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; CAL98532.1; -; Genomic_DNA.
DR   RefSeq; WP_011835704.1; NZ_WJVF01000007.1.
DR   PDB; 4DVE; X-ray; 2.09 A; A/B/C=2-188.
DR   PDBsum; 4DVE; -.
DR   AlphaFoldDB; A2RMJ9; -.
DR   SMR; A2RMJ9; -.
DR   STRING; 416870.llmg_1964; -.
DR   TCDB; 3.A.1.25.4; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; CAL98532; CAL98532; llmg_1964.
DR   KEGG; llm:llmg_1964; -.
DR   eggNOG; COG1268; Bacteria.
DR   HOGENOM; CLU_077931_0_1_9; -.
DR   OMA; AGYLWSY; -.
DR   PhylomeDB; A2RMJ9; -.
DR   BioCyc; LLAC416870:LLMG_RS09825-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   3D-structure; Cell membrane; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..189
FT                   /note="Biotin transporter BioY"
FT                   /id="PRO_0000409004"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   HELIX           3..23
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           42..70
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           83..86
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           90..109
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           118..129
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           131..145
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           149..155
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           156..159
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           160..179
FT                   /evidence="ECO:0007829|PDB:4DVE"
FT   HELIX           184..187
FT                   /evidence="ECO:0007829|PDB:4DVE"
SQ   SEQUENCE   189 AA;  20479 MW;  427632C8C0E7CE13 CRC64;
     MTNNQKVKTL TYSAFMTAFI IILGFLPGIP IGFIPVPIIL QNMGIMMAGG LLGPKYGTIS
     VGAFLALALI GLPVLTGGNG GAASFLGPSG GYRIAWLFTP FLIGFFLKKL KITTSQNWFG
     ELIIVLLFGV IFVDFVGAIW LSFQSNIPLL TSLISNLVFI PGDCIKAILT VVIVRRLRKQ
     GGFELYFRK