LPTG_ECOLI
ID LPTG_ECOLI Reviewed; 360 AA.
AC P0ADC6; P39341; Q2M647;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Lipopolysaccharide export system permease protein LptG;
GN Name=lptG; Synonyms=yjgQ; OrderedLocusNames=b4262, JW5760;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [5]
RP FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=18375759; DOI=10.1073/pnas.0801196105;
RA Ruiz N., Gronenberg L.S., Kahne D., Silhavy T.J.;
RT "Identification of two inner-membrane proteins required for the transport
RT of lipopolysaccharide to the outer membrane of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5537-5542(2008).
RN [6]
RP SUBUNIT, AND INTERACTION WITH LPTB AND LPTF.
RX PubMed=19500581; DOI=10.1016/j.febslet.2009.05.051;
RA Narita S., Tokuda H.;
RT "Biochemical characterization of an ABC transporter LptBFGC complex
RT required for the outer membrane sorting of lipopolysaccharides.";
RL FEBS Lett. 583:2160-2164(2009).
CC -!- FUNCTION: Part of the ABC transporter complex LptBFG involved in the
CC translocation of lipopolysaccharide (LPS) from the inner membrane to
CC the outer membrane. {ECO:0000269|PubMed:18375759}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. The LptBFG transporter is composed of two ATP-binding proteins
CC (LptB) and two transmembrane proteins (LptF and LptG).
CC {ECO:0000269|PubMed:19500581}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the LptF/LptG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97159.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97159.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77219.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78259.1; -; Genomic_DNA.
DR RefSeq; NP_418683.4; NC_000913.3.
DR RefSeq; WP_001295681.1; NZ_STEB01000013.1.
DR PDB; 6MHU; EM; 4.00 A; G=1-360.
DR PDB; 6MHZ; EM; 4.10 A; G=1-360.
DR PDB; 6MI7; EM; 4.20 A; G=1-360.
DR PDB; 6MI8; EM; 4.30 A; G=1-360.
DR PDBsum; 6MHU; -.
DR PDBsum; 6MHZ; -.
DR PDBsum; 6MI7; -.
DR PDBsum; 6MI8; -.
DR AlphaFoldDB; P0ADC6; -.
DR SMR; P0ADC6; -.
DR BioGRID; 4262728; 247.
DR ComplexPortal; CPX-3861; lptBFG LPS ABC transporter complex.
DR IntAct; P0ADC6; 1.
DR MINT; P0ADC6; -.
DR STRING; 511145.b4262; -.
DR TCDB; 1.B.42.1.2; the outer membrane lipopolysaccharide export porin (lps-ep) family.
DR jPOST; P0ADC6; -.
DR PaxDb; P0ADC6; -.
DR PRIDE; P0ADC6; -.
DR DNASU; 945324; -.
DR EnsemblBacteria; AAC77219; AAC77219; b4262.
DR EnsemblBacteria; BAE78259; BAE78259; BAE78259.
DR GeneID; 66671819; -.
DR GeneID; 945324; -.
DR KEGG; ecj:JW5760; -.
DR KEGG; eco:b4262; -.
DR PATRIC; fig|1411691.4.peg.2441; -.
DR EchoBASE; EB2425; -.
DR eggNOG; COG0795; Bacteria.
DR HOGENOM; CLU_028799_1_1_6; -.
DR InParanoid; P0ADC6; -.
DR OMA; WFTSKLA; -.
DR PhylomeDB; P0ADC6; -.
DR BioCyc; EcoCyc:G7889-MON; -.
DR BioCyc; MetaCyc:G7889-MON; -.
DR PRO; PR:P0ADC6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1990351; C:transporter complex; IDA:EcoCyc.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IC:ComplexPortal.
DR GO; GO:0015920; P:lipopolysaccharide transport; IDA:ComplexPortal.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR030923; LptG.
DR InterPro; IPR005495; LptG/LptF_permease.
DR PANTHER; PTHR33529; PTHR33529; 1.
DR Pfam; PF03739; LptF_LptG; 1.
DR TIGRFAMs; TIGR04408; LptG_lptG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..360
FT /note="Lipopolysaccharide export system permease protein
FT LptG"
FT /id="PRO_0000169776"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..63
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..278
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 360 AA; 39619 MW; 72BA4E01FE6167C9 CRC64;
MQPFGVLDRY IGKTIFTTIM MTLFMLVSLS GIIKFVDQLK KAGQGSYDAL GAGMYTLLSV
PKDVQIFFPM AALLGALLGL GMLAQRSELV VMQASGFTRM QVALSVMKTA IPLVLLTMAI
GEWVAPQGEQ MARNYRAQAM YGGSLLSTQQ GLWAKDGNNF VYIERVKGDE ELGGISIYAF
NENRRLQSVR YAATAKFDPE HKVWRLSQVD ESDLTNPKQI TGSQTVSGTW KTNLTPDKLG
VVALDPDALS ISGLHNYVKY LKSSGQDAGR YQLNMWSKIF QPLSVAVMML MALSFIFGPL
RSVPMGVRVV TGISFGFVFY VLDQIFGPLT LVYGIPPIIG ALLPSASFFL ISLWLLMRKS
