LPTB_ECOLI
ID LPTB_ECOLI Reviewed; 241 AA.
AC P0A9V1; P31220; Q2M911;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Lipopolysaccharide export system ATP-binding protein LptB;
DE EC=7.5.2.-;
GN Name=lptB; Synonyms=yhbG; OrderedLocusNames=b3201, JW3168;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8444818; DOI=10.1128/jb.175.5.1550-1551.1993;
RA Imaishi H., Gomada M., Inouye S., Nakazawa A.;
RT "Physical map location of the rpoN gene of Escherichia coli.";
RL J. Bacteriol. 175:1550-1551(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7876255; DOI=10.1074/jbc.270.9.4822;
RA Powell B.S., Court D.L., Inada T., Nakamura Y., Michotey V., Cui X.,
RA Reizer A., Saier M.H. Jr., Reizer J.;
RT "Novel proteins of the phosphotransferase system encoded within the rpoN
RT operon of Escherichia coli. Enzyme IIANtr affects growth on organic
RT nitrogen and the conditional lethality of an erats mutant.";
RL J. Biol. Chem. 270:4822-4839(1995).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [7]
RP FUNCTION IN LPS BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RX PubMed=16765569; DOI=10.1016/j.resmic.2005.11.014;
RA Sperandeo P., Pozzi C., Deho G., Polissi A.;
RT "Non-essential KDO biosynthesis and new essential cell envelope biogenesis
RT genes in the Escherichia coli yrbG-yhbG locus.";
RL Res. Microbiol. 157:547-558(2006).
RN [8]
RP FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT, AND INDUCTION.
RX PubMed=17056748; DOI=10.1128/jb.01126-06;
RA Sperandeo P., Cescutti R., Villa R., Di Benedetto C., Candia D., Deho G.,
RA Polissi A.;
RT "Characterization of lptA and lptB, two essential genes implicated in
RT lipopolysaccharide transport to the outer membrane of Escherichia coli.";
RL J. Bacteriol. 189:244-253(2007).
RN [9]
RP FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=18424520; DOI=10.1128/jb.00270-08;
RA Sperandeo P., Lau F.K., Carpentieri A., De Castro C., Molinaro A., Deho G.,
RA Silhavy T.J., Polissi A.;
RT "Functional analysis of the protein machinery required for transport of
RT lipopolysaccharide to the outer membrane of Escherichia coli.";
RL J. Bacteriol. 190:4460-4469(2008).
RN [10]
RP SUBUNIT, AND INTERACTION WITH LPTF AND LPTG.
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. Probably responsible for energy coupling to the
CC transport system. {ECO:0000269|PubMed:16765569,
CC ECO:0000269|PubMed:17056748, ECO:0000269|PubMed:18424520}.
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: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell
CC inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane
CC protein {ECO:0000269|PubMed:16079137}; Cytoplasmic side
CC {ECO:0000269|PubMed:16079137}.
CC -!- INDUCTION: Transcriptionally regulated by sigma-E factor.
CC {ECO:0000269|PubMed:17056748}.
CC -!- DISRUPTION PHENOTYPE: Results in an earlier growth arrest and onset of
CC cell lethality. {ECO:0000269|PubMed:16765569}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Outer membrane
CC lipopolysaccharide export (TC 1.B.42) family. {ECO:0000305}.
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DR EMBL; D12938; BAA02314.1; -; Genomic_DNA.
DR EMBL; U12684; AAB60162.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58003.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76233.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77245.1; -; Genomic_DNA.
DR PIR; C65111; C65111.
DR RefSeq; NP_417668.1; NC_000913.3.
DR RefSeq; WP_000224099.1; NZ_STEB01000012.1.
DR PDB; 4P31; X-ray; 2.05 A; A/B=2-241.
DR PDB; 4P32; X-ray; 1.55 A; A/B=2-241.
DR PDB; 4P33; X-ray; 1.65 A; A/B=2-241.
DR PDB; 6B89; X-ray; 2.00 A; A/B=2-241.
DR PDB; 6B8B; X-ray; 1.95 A; A=2-241.
DR PDB; 6MBN; X-ray; 1.96 A; A/B=2-241.
DR PDB; 6MGF; X-ray; 2.98 A; A=1-241.
DR PDB; 6MHU; EM; 4.00 A; A/B=1-241.
DR PDB; 6MHZ; EM; 4.10 A; A/B=1-241.
DR PDB; 6MI7; EM; 4.20 A; A/B=1-241.
DR PDB; 6MI8; EM; 4.30 A; A/B=1-241.
DR PDBsum; 4P31; -.
DR PDBsum; 4P32; -.
DR PDBsum; 4P33; -.
DR PDBsum; 6B89; -.
DR PDBsum; 6B8B; -.
DR PDBsum; 6MBN; -.
DR PDBsum; 6MGF; -.
DR PDBsum; 6MHU; -.
DR PDBsum; 6MHZ; -.
DR PDBsum; 6MI7; -.
DR PDBsum; 6MI8; -.
DR AlphaFoldDB; P0A9V1; -.
DR SMR; P0A9V1; -.
DR ComplexPortal; CPX-3861; lptBFG LPS ABC transporter complex.
DR DIP; DIP-31876N; -.
DR IntAct; P0A9V1; 5.
DR MINT; P0A9V1; -.
DR STRING; 511145.b3201; -.
DR TCDB; 1.B.42.1.2; the outer membrane lipopolysaccharide export porin (lps-ep) family.
DR jPOST; P0A9V1; -.
DR PaxDb; P0A9V1; -.
DR PRIDE; P0A9V1; -.
DR EnsemblBacteria; AAC76233; AAC76233; b3201.
DR EnsemblBacteria; BAE77245; BAE77245; BAE77245.
DR GeneID; 67415965; -.
DR GeneID; 947725; -.
DR KEGG; ecj:JW3168; -.
DR KEGG; eco:b3201; -.
DR PATRIC; fig|1411691.4.peg.3530; -.
DR EchoBASE; EB1631; -.
DR eggNOG; COG1137; Bacteria.
DR HOGENOM; CLU_000604_1_2_6; -.
DR InParanoid; P0A9V1; -.
DR OMA; LPMYQRA; -.
DR PhylomeDB; P0A9V1; -.
DR BioCyc; EcoCyc:YHBG-MON; -.
DR BioCyc; MetaCyc:YHBG-MON; -.
DR BRENDA; 7.5.2.5; 2026.
DR PRO; PR:P0A9V1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 CDD; cd03218; ABC_YhbG; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR032823; BCA_ABC_TP_C.
DR InterPro; IPR030921; LPS_export_LptB.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF12399; BCA_ABC_TP_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR04406; LPS_export_lptB; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..241
FT /note="Lipopolysaccharide export system ATP-binding protein
FT LptB"
FT /id="PRO_0000093178"
FT DOMAIN 4..237
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 55..57
FT /note="RDA -> ARC (in Ref. 1; AAB60162/BAA02314)"
FT /evidence="ECO:0000305"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:4P32"
FT STRAND 16..27
FT /evidence="ECO:0007829|PDB:4P32"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:4P32"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:4P32"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4P32"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6MBN"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:4P32"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:4P32"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:4P32"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:4P32"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:4P32"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:4P32"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4P32"
SQ SEQUENCE 241 AA; 26801 MW; 6041495BDDCDFA72 CRC64;
MATLTAKNLA KAYKGRRVVE DVSLTVNSGE IVGLLGPNGA GKTTTFYMVV GIVPRDAGNI
IIDDDDISLL PLHARARRGI GYLPQEASIF RRLSVYDNLM AVLQIRDDLS AEQREDRANE
LMEEFHIEHL RDSMGQSLSG GERRRVEIAR ALAANPKFIL LDEPFAGVDP ISVIDIKRII
EHLRDSGLGV LITDHNVRET LAVCERAYIV SQGHLIAHGT PTEILQDEHV KRVYLGEDFR
L
