ECFT_LEVBA
ID ECFT_LEVBA Reviewed; 266 AA.
AC Q03PY7;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=LVIS_1660;
OS Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS 1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=387344;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC 947 / NCTC 947;
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000416; ABJ64735.1; -; Genomic_DNA.
DR RefSeq; WP_011668469.1; NC_008497.1.
DR PDB; 4HUQ; X-ray; 3.00 A; T=1-266.
DR PDB; 4HZU; X-ray; 3.53 A; T=1-266.
DR PDB; 4RFS; X-ray; 3.23 A; T=1-266.
DR PDBsum; 4HUQ; -.
DR PDBsum; 4HZU; -.
DR PDBsum; 4RFS; -.
DR AlphaFoldDB; Q03PY7; -.
DR SMR; Q03PY7; -.
DR DIP; DIP-60220N; -.
DR IntAct; Q03PY7; 4.
DR STRING; 387344.LVIS_1660; -.
DR TCDB; 3.A.1.26.9; the atp-binding cassette (abc) superfamily.
DR TCDB; 3.A.1.28.2; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ABJ64735; ABJ64735; LVIS_1660.
DR KEGG; lbr:LVIS_1660; -.
DR eggNOG; COG0619; Bacteria.
DR HOGENOM; CLU_056469_2_2_9; -.
DR OMA; NNIMIGR; -.
DR OrthoDB; 1479665at2; -.
DR Proteomes; UP000001652; 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 3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..266
FT /note="Energy-coupling factor transporter transmembrane
FT protein EcfT"
FT /id="PRO_0000408990"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01461"
FT TRANSMEM 152..172
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"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:4HUQ"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:4HUQ"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:4HUQ"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:4HUQ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4HUQ"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:4HUQ"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:4RFS"
FT HELIX 104..129
FT /evidence="ECO:0007829|PDB:4HUQ"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:4HUQ"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4RFS"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4HUQ"
FT HELIX 154..183
FT /evidence="ECO:0007829|PDB:4HUQ"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4RFS"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:4HUQ"
FT HELIX 202..225
FT /evidence="ECO:0007829|PDB:4HUQ"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4HUQ"
FT HELIX 244..261
FT /evidence="ECO:0007829|PDB:4HUQ"
SQ SEQUENCE 266 AA; 30292 MW; D086E5529FE243AF CRC64;
MSNFIFGRYL PLDSVVHRLD PRAKLMLSFC YIIVVFLANN IWSYAILIAF TVGAILSSKI
SLGFFLKGIR PLLWLIVFTV VLQLLFSPAG GHTYFHWAFI NVTQDGLINA GYIFVRFLLI
IMMSTLLTLS TQPLDIATGL ASLMKPLRWV KVPVDTLAMM LSIALRFVPT LMDEATKIMN
AQRARGVDFG EGGLFKQAKS LIPLMVPLFM SAFNRAEDLS TAMEARGYQD SEHRSQYRIL
TWQRRDTVTW LLFLLGFVAI LIFRHW