ECFT_RUMCH
ID ECFT_RUMCH Reviewed; 267 AA.
AC B8I813;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=Ccel_0792;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001348; ACL75170.1; -; Genomic_DNA.
DR RefSeq; WP_015924332.1; NC_011898.1.
DR AlphaFoldDB; B8I813; -.
DR SMR; B8I813; -.
DR STRING; 394503.Ccel_0792; -.
DR EnsemblBacteria; ACL75170; ACL75170; Ccel_0792.
DR KEGG; cce:Ccel_0792; -.
DR eggNOG; COG0619; Bacteria.
DR HOGENOM; CLU_056469_2_2_9; -.
DR OMA; MKAQMSR; -.
DR OrthoDB; 1479665at2; -.
DR Proteomes; UP000001349; 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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..267
FT /note="Energy-coupling factor transporter transmembrane
FT protein EcfT"
FT /id="PRO_0000408986"
FT TRANSMEM 26..46
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 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
SQ SEQUENCE 267 AA; 30336 MW; A1E76053C37D1696 CRC64;
MIRDITIGQY VPGNSLLHKA DPRTKIILTF IMMIFIFLIN TYWGYLLLTL FTAITVVSSN
IPVKFVLKGL KPILFIVVFA GIINIFMIKG TVIWSWGFLS ITYEGINVAI KMAIRLFLLI
ITASLLTYTT TPIALTDAIE NLLAPLKRIK VPVHEIAMMM TIALRFIPTL LDETDKIIKA
QSSRGADFDS GNMIERAKSF IPVLIPLFIS AFRRADELAT AMEARCYRGS EGRTRMKQLR
FTRFDVLVTG ITVVFMTWVI LMEYVFF