LPTA_ECOLI
ID LPTA_ECOLI Reviewed; 185 AA.
AC P0ADV1; P38685; Q2M912;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Lipopolysaccharide export system protein LptA {ECO:0000255|HAMAP-Rule:MF_01914};
DE Flags: Precursor;
GN Name=lptA {ECO:0000255|HAMAP-Rule:MF_01914}; Synonyms=yhbN;
GN OrderedLocusNames=b3200, JW3167;
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 / 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 [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 PROTEIN SEQUENCE OF 28-39.
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 [5]
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 [6]
RP FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT, SUBCELLULAR LOCATION, AND
RP 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 [7]
RP FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT, AND SUBUNIT.
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 [8]
RP FUNCTION IN LIPOPOLYSACCHARIDE TRANSPORT, SUBUNIT, SUBCELLULAR LOCATION,
RP AND LIPID A-BINDING.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=18480051; DOI=10.1074/jbc.m802503200;
RA Tran A.X., Trent M.S., Whitfield C.;
RT "The LptA protein of Escherichia coli is a periplasmic lipid A-binding
RT protein involved in the lipopolysaccharide export pathway.";
RL J. Biol. Chem. 283:20342-20349(2008).
RN [9]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=20446753; DOI=10.1021/bi100493e;
RA Chng S.S., Gronenberg L.S., Kahne D.;
RT "Proteins required for lipopolysaccharide assembly in Escherichia coli form
RT a transenvelope complex.";
RL Biochemistry 49:4565-4567(2010).
RN [10]
RP INTERACTION WITH LPTC.
RC STRAIN=K12;
RX PubMed=21195693; DOI=10.1016/j.bbrc.2010.12.121;
RA Bowyer A., Baardsnes J., Ajamian E., Zhang L., Cygler M.;
RT "Characterization of interactions between LPS transport proteins of the Lpt
RT system.";
RL Biochem. Biophys. Res. Commun. 404:1093-1098(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH LPTC.
RX PubMed=21169485; DOI=10.1128/jb.01037-10;
RA Sperandeo P., Villa R., Martorana A.M., Samalikova M., Grandori R.,
RA Deho G., Polissi A.;
RT "New insights into the Lpt machinery for lipopolysaccharide transport to
RT the cell surface: LptA-LptC interaction and LptA stability as sensors of a
RT properly assembled transenvelope complex.";
RL J. Bacteriol. 193:1042-1053(2011).
RN [12]
RP SUBUNIT, INTERACTION WITH LPTC AND LPTD, AND DOMAIN.
RX PubMed=22668317; DOI=10.1021/bi300592c;
RA Freinkman E., Okuda S., Ruiz N., Kahne D.;
RT "Regulated assembly of the transenvelope protein complex required for
RT lipopolysaccharide export.";
RL Biochemistry 51:4800-4806(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 27-185, SUBUNIT, AND MUTAGENESIS
RP OF ILE-36; ILE-38; ARG-76 AND PHE-95.
RC STRAIN=K12;
RX PubMed=18534617; DOI=10.1016/j.jmb.2008.04.045;
RA Suits M.D.L., Sperandeo P., Deho G., Polissi A., Jia Z.;
RT "Novel structure of the conserved Gram-negative lipopolysaccharide
RT transport protein A and mutagenesis analysis.";
RL J. Mol. Biol. 380:476-488(2008).
CC -!- FUNCTION: Involved in the assembly of lipopolysaccharide (LPS).
CC Required for the translocation of LPS from the inner membrane to the
CC outer membrane. May form a bridge between the inner membrane and the
CC outer membrane, via interactions with LptC and LptD, thereby
CC facilitating LPS transfer across the periplasm. {ECO:0000255|HAMAP-
CC Rule:MF_01914, ECO:0000269|PubMed:16765569,
CC ECO:0000269|PubMed:17056748, ECO:0000269|PubMed:18424520,
CC ECO:0000269|PubMed:18480051, ECO:0000269|PubMed:21169485}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. Can form head-to-tail homodimers and oligomers. Interacts with
CC LptC, LptD and with the lipid A domain of LPS. {ECO:0000255|HAMAP-
CC Rule:MF_01914, ECO:0000269|PubMed:18424520,
CC ECO:0000269|PubMed:18480051, ECO:0000269|PubMed:18534617,
CC ECO:0000269|PubMed:20446753, ECO:0000269|PubMed:21169485,
CC ECO:0000269|PubMed:21195693, ECO:0000269|PubMed:22668317}.
CC -!- INTERACTION:
CC P0ADV1; P0ADV9: lptC; NbExp=3; IntAct=EBI-1132001, EBI-1131969;
CC P0ADV1; P31554: lptD; NbExp=4; IntAct=EBI-1132001, EBI-549369;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01914,
CC ECO:0000269|PubMed:17056748, ECO:0000269|PubMed:18480051,
CC ECO:0000269|PubMed:20446753}. Note=Associates with both the inner
CC membrane and the outer membrane.
CC -!- INDUCTION: Transcriptionally regulated by sigma-E factor.
CC {ECO:0000269|PubMed:17056748}.
CC -!- DOMAIN: The N-terminal domain interacts with LptC, at the inner
CC membrane, and the C-terminal domain interacts with LptD, at the outer
CC membrane. {ECO:0000269|PubMed:22668317}.
CC -!- DISRUPTION PHENOTYPE: Results in an earlier growth arrest and onset of
CC cell lethality. {ECO:0000269|PubMed:16765569}.
CC -!- SIMILARITY: Belongs to the LptA family. {ECO:0000255|HAMAP-
CC Rule:MF_01914}.
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DR EMBL; U12684; AAB60161.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58002.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76232.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77244.1; -; Genomic_DNA.
DR PIR; B65111; B65111.
DR RefSeq; NP_417667.1; NC_000913.3.
DR RefSeq; WP_000669785.1; NZ_STEB01000012.1.
DR PDB; 2R19; X-ray; 2.16 A; A/B=27-185.
DR PDB; 2R1A; X-ray; 3.26 A; A/B/C/D/E/F/G/H=27-185.
DR PDB; 6GD5; NMR; -; A=28-144.
DR PDBsum; 2R19; -.
DR PDBsum; 2R1A; -.
DR PDBsum; 6GD5; -.
DR AlphaFoldDB; P0ADV1; -.
DR SMR; P0ADV1; -.
DR BioGRID; 4259280; 249.
DR DIP; DIP-12262N; -.
DR IntAct; P0ADV1; 6.
DR STRING; 511145.b3200; -.
DR TCDB; 1.B.42.1.2; the outer membrane lipopolysaccharide export porin (lps-ep) family.
DR jPOST; P0ADV1; -.
DR PaxDb; P0ADV1; -.
DR PRIDE; P0ADV1; -.
DR EnsemblBacteria; AAC76232; AAC76232; b3200.
DR EnsemblBacteria; BAE77244; BAE77244; BAE77244.
DR GeneID; 67415966; -.
DR GeneID; 947920; -.
DR KEGG; ecj:JW3167; -.
DR KEGG; eco:b3200; -.
DR PATRIC; fig|1411691.4.peg.3531; -.
DR EchoBASE; EB2502; -.
DR eggNOG; COG1934; Bacteria.
DR HOGENOM; CLU_095993_2_1_6; -.
DR InParanoid; P0ADV1; -.
DR OMA; VPTQQME; -.
DR PhylomeDB; P0ADV1; -.
DR BioCyc; EcoCyc:YHBN-MON; -.
DR BioCyc; MetaCyc:YHBN-MON; -.
DR BRENDA; 2.7.8.43; 2026.
DR EvolutionaryTrace; P0ADV1; -.
DR PRO; PR:P0ADV1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
DR GO; GO:1990351; C:transporter complex; IDA:EcoCyc.
DR GO; GO:0017089; F:glycolipid transfer activity; IMP:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:InterPro.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0015920; P:lipopolysaccharide transport; IMP:EcoCyc.
DR HAMAP; MF_01914; LPS_assembly_LptA; 1.
DR InterPro; IPR014340; LptA.
DR InterPro; IPR005653; OstA-like_N.
DR Pfam; PF03968; LptD_N; 1.
DR TIGRFAMs; TIGR03002; outer_YhbN_LptA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Periplasm; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01914,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 28..185
FT /note="Lipopolysaccharide export system protein LptA"
FT /id="PRO_0000013914"
FT REGION 166..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 36
FT /note="I->D,E: No change in activity."
FT /evidence="ECO:0000269|PubMed:18534617"
FT MUTAGEN 38
FT /note="I->D: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:18534617"
FT MUTAGEN 38
FT /note="I->E: No change in activity."
FT /evidence="ECO:0000269|PubMed:18534617"
FT MUTAGEN 76
FT /note="R->D,E: No change in activity."
FT /evidence="ECO:0000269|PubMed:18534617"
FT MUTAGEN 95
FT /note="F->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:18534617"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:2R19"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 51..62
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:6GD5"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2R19"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:2R19"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2R19"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2R1A"
SQ SEQUENCE 185 AA; 20127 MW; BA69198479C68DC1 CRC64;
MKFKTNKLSL NLVLASSLLA ASIPAFAVTG DTDQPIHIES DQQSLDMQGN VVTFTGNVIV
TQGTIKINAD KVVVTRPGGE QGKEVIDGYG KPATFYQMQD NGKPVEGHAS QMHYELAKDF
VVLTGNAYLQ QVDSNIKGDK ITYLVKEQKM QAFSDKGKRV TTVLVPSQLQ DKNNKGQTPA
QKKGN
