ID   ECFT_STRE4              Reviewed;         269 AA.
AC   C0MBF3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Energy-coupling factor transporter transmembrane protein EcfT {ECO:0000255|HAMAP-Rule:MF_01461};
DE            Short=ECF transporter T component EcfT {ECO:0000255|HAMAP-Rule:MF_01461};
GN   Name=ecfT {ECO:0000255|HAMAP-Rule:MF_01461}; OrderedLocusNames=SEQ_2213;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- FUNCTION: Transmembrane (T) component of an energy-coupling factor
CC       (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF
CC       transporter provides the energy necessary to transport a number of
CC       different substrates. {ECO:0000255|HAMAP-Rule:MF_01461}.
CC   -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC       complex composed of 2 membrane-embedded substrate-binding proteins (S
CC       component), 2 ATP-binding proteins (A component) and 2 transmembrane
CC       proteins (T component). May be able to interact with more than 1 S
CC       component at a time (By similarity). {ECO:0000255|HAMAP-Rule:MF_01461}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01461};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01461}.
CC   -!- SIMILARITY: Belongs to the energy-coupling factor EcfT family.
CC       {ECO:0000255|HAMAP-Rule:MF_01461}.
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DR   EMBL; FM204883; CAW95622.1; -; Genomic_DNA.
DR   RefSeq; WP_015898702.1; NC_012471.1.
DR   AlphaFoldDB; C0MBF3; -.
DR   SMR; C0MBF3; -.
DR   EnsemblBacteria; CAW95622; CAW95622; SEQ_2213.
DR   KEGG; seu:SEQ_2213; -.
DR   HOGENOM; CLU_056469_2_2_9; -.
DR   OMA; MKAQMSR; -.
DR   OrthoDB; 1479665at2; -.
DR   Proteomes; UP000001365; 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:UniProtKB-UniRule.
DR   HAMAP; MF_01461; EcfT; 1.
DR   InterPro; IPR003339; ABC/ECF_trnsptr_transmembrane.
DR   InterPro; IPR024919; EcfT.
DR   Pfam; PF02361; CbiQ; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..269
FT                   /note="Energy-coupling factor transporter transmembrane
FT                   protein EcfT"
FT                   /id="PRO_0000409001"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
SQ   SEQUENCE   269 AA;  30172 MW;  82B008B19ECB9907 CRC64;
     MDKLILGRYI PGNSIIHRLD PRSKLLAMII YIIIIFWANN VVTNLLLLAF TLLLIFLSQI
     KWSFFFNGVK PMIGIILFTT LFQVFFTQGG SVLFQLGIIK ITSLGLSQAI LIFMRFVLII
     FFSTLLTLTT TPLSLSDAVE ALLKPLVRFK VPAHEIGLML SLSLRFVPTL MDDTTRIMNA
     QKARGVDFGE GNLIQKVKSI IPILIPLFAS SFKRADALAI AMEARGYQGG DSRTKYRLLS
     WQLKDTLAII LVVILGIFLF CLKSPSRLT