ID   ECFT_LACLM              Reviewed;         266 AA.
AC   A2RI03;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Energy-coupling factor transporter transmembrane protein EcfT;
DE            Short=ECF transporter T component EcfT;
GN   Name=ecfT; OrderedLocusNames=llmg_0289;
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, TRANSPORT SUBSTRATES, AND EXPRESSION IN
RP   E.COLI AND L.LACTIS.
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: Part of a common energy-coupling factor (ECF) ABC-transporter
CC       complex. Unlike classic ABC transporters this ECF transporter provides
CC       the energy necessary to transport a number of different substrates. In
CC       this organism these probably include biotin, thiamine precursor,
CC       niacin, pantothenic acid, queuosine precursor, riboflavin and thiamine.
CC       Uptake of niacin or riboflavin into proteosomes containing EcfA1A2T and
CC       Niax or RibU has been demonstrated. Uptake requires hydrolyzable Mg-ATP
CC       and is substrate-specific; NiaX-containing proteosomes did not
CC       transport riboflavin.
CC   -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC       complex possibly composed of 2 membrane-embedded substrate-binding
CC       proteins (S component), 2 ATP-binding proteins (A component) and 2
CC       transmembrane proteins (T component). In L.lactis forms a stable
CC       complex with EcfA' and EcfT and S components. In E.coli forms a stable
CC       complex with EcfA, EcfA' and individually with 3 tested S components
CC       (BioY, NiaX and ThiT) with a stoichiometry of 1:1:1:1. The core ECF
CC       complex interacts with a number of substrate-specific binding
CC       components, including BioY, BioY2, HmpT, NiaX, PanT, QueT, RibU and
CC       ThiT. May be able to interact with more than 1 S component at a time.
CC       {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 energy-coupling factor EcfT family.
CC       {ECO:0000305}.
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DR   EMBL; AM406671; CAL96896.1; -; Genomic_DNA.
DR   RefSeq; WP_011675312.1; NZ_WJVF01000001.1.
DR   AlphaFoldDB; A2RI03; -.
DR   SMR; A2RI03; -.
DR   STRING; 416870.llmg_0289; -.
DR   TCDB; 3.A.1.25.4; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; CAL96896; CAL96896; llmg_0289.
DR   KEGG; llm:llmg_0289; -.
DR   eggNOG; COG0619; Bacteria.
DR   HOGENOM; CLU_056469_2_2_9; -.
DR   OMA; MKAQMSR; -.
DR   PhylomeDB; A2RI03; -.
DR   BioCyc; LLAC416870:LLMG_RS01510-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:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:GO_Central.
DR   HAMAP; MF_01461; EcfT; 1.
DR   InterPro; IPR003339; ABC/ECF_trnsptr_transmembrane.
DR   InterPro; IPR024919; EcfT.
DR   Pfam; PF02361; CbiQ; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..266
FT                   /note="Energy-coupling factor transporter transmembrane
FT                   protein EcfT"
FT                   /id="PRO_0000408994"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   266 AA;  30161 MW;  5581EC28032DFCC6 CRC64;
     MQNMLMGRYI PGDSIIHRMD PRSKLLVMIA FVVIIFLAHD WLGYLLLVLY TLAGVLLSKI
     SVSYFLRGLR PMIGLILFTV IFQMLFTNGQ HVIFSLWFIK ISTESLINAV YIFFRFVLII
     FMSTILTLTT PPLTLADGIE KGLGPLKKIK VPVHELGLML SISLRFIPTL MDDTTMIMNA
     QKARGMDFGE GNLLKKIKSV IPILIPLFVS SFRRADDLAV AMESRGYQGG DGRTKYRQLK
     WQSRDSLLVV SIIIMTILLI LWSKVS