ECFT_LEUMM
ID ECFT_LEUMM Reviewed; 267 AA.
AC Q03ZL4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Energy-coupling factor transporter transmembrane protein EcfT;
DE Short=ECF transporter T component EcfT;
GN Name=ecfT; OrderedLocusNames=LEUM_0227;
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
RN [2]
RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION,
RP SUBSTRATES, AND EXPRESSION IN E.COLI.
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX PubMed=18931129; DOI=10.1128/jb.01208-08;
RA Rodionov D.A., Hebbeln P., Eudes A., ter Beek J., Rodionova I.A.,
RA Erkens G.B., Slotboom D.J., Gelfand M.S., Osterman A.L., Hanson A.D.,
RA Eitinger T.;
RT "A novel class of modular transporters for vitamins in prokaryotes.";
RL J. Bacteriol. 191:42-51(2009).
RN [3]
RP FUNCTION AS A TRANSPORT COMPONENT, SUBCELLULAR LOCATION, POSSIBLE TOPOLOGY,
RP AND MUTAGENESIS OF ARG-184 AND ARG-225.
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX PubMed=19717603; DOI=10.1128/jb.00965-09;
RA Neubauer O., Alfandega A., Schoknecht J., Sternberg U., Pohlmann A.,
RA Eitinger T.;
RT "Two essential arginine residues in the T components of energy-coupling
RT factor transporters.";
RL J. Bacteriol. 191:6482-6488(2009).
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
CC including 5-formyltetrahydrofolate, pantothenate and riboflavin. Upon
CC expression of the complex plus FolT in E.coli allows 5-
CC formyltetrahydrofolate uptake; 5-formyltetrahydrofolate is not taken up
CC in the absence of FolT or the EcfA1A2T complex.
CC {ECO:0000269|PubMed:18931129, ECO:0000269|PubMed:19717603}.
CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC complex probably composed of 2 membrane-embedded substrate-binding
CC proteins (S component), 2 ATP-binding proteins (A component) and 2
CC transmembrane proteins (T component). This complex interacts with a
CC number of substrate-specific components, including FolT, PanT and RibU
CC for 5-formyltetrahydrofolate, pantothenate and riboflavin respectively.
CC May be able to interact with more than 1 S component at a time.
CC {ECO:0000269|PubMed:18931129}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:18931129,
CC ECO:0000305|PubMed:19717603}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:18931129, ECO:0000305|PubMed:19717603}.
CC -!- SIMILARITY: Belongs to the energy-coupling factor EcfT family.
CC {ECO:0000305}.
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DR EMBL; CP000414; ABJ61358.1; -; Genomic_DNA.
DR RefSeq; WP_011679142.1; NC_008531.1.
DR AlphaFoldDB; Q03ZL4; -.
DR SMR; Q03ZL4; -.
DR STRING; 203120.LEUM_0227; -.
DR EnsemblBacteria; ABJ61358; ABJ61358; LEUM_0227.
DR GeneID; 61177294; -.
DR KEGG; lme:LEUM_0227; -.
DR eggNOG; COG0619; Bacteria.
DR HOGENOM; CLU_056469_2_2_9; -.
DR OMA; NNIMIGR; -.
DR OrthoDB; 1479665at2; -.
DR Proteomes; UP000000362; 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 1: Evidence at protein level;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..267
FT /note="Energy-coupling factor transporter transmembrane
FT protein EcfT"
FT /id="PRO_0000408996"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 184
FT /note="R->E: Abolishes folate and pantothenate uptake,
FT whole ECF complex stably associates with FolT, PanT or
FT RibU."
FT /evidence="ECO:0000269|PubMed:19717603"
FT MUTAGEN 225
FT /note="R->E: Abolishes folate and pantothenate uptake, EcfT
FT does not assemble with the A and S components."
FT /evidence="ECO:0000269|PubMed:19717603"
SQ SEQUENCE 267 AA; 30003 MW; E121FDC5AE48602F CRC64;
MNNIMIGRFV PGDSWIHRLD PRTKMIGTFI FIFVMLWSTS WATYAWSAAF VVLAIRLTKQ
PFRLYWDGLK PIFWLILFTV VLQLFFTPGT PVLLHAGPLK VTIPGIINAI YVMIRFVLII
LMSTILTLTT PPTSIANALE SLLKPLKKIH VPVAELSLML SIALRFVPLL MDETQKIMNA
QKSRGMSFST GGPIKRAKAI VPLLIPLFVG ALQRALDLAN AMEVRGFQDA TQRTKYRVLS
YGSNDRSAFI GLIGFTIIFI GINFFIK
