LPTC_ECOLI
ID LPTC_ECOLI Reviewed; 191 AA.
AC P0ADV9; P45397; Q2M913;
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 LptC {ECO:0000255|HAMAP-Rule:MF_01915};
GN Name=lptC {ECO:0000255|HAMAP-Rule:MF_01915}; Synonyms=yrbK;
GN OrderedLocusNames=b3199, JW3166;
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-191.
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 [4]
RP PROTEIN SEQUENCE OF 1-5, AND INTERACTION WITH LPTBFG.
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).
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, AND SUBCELLULAR LOCATION.
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 [7]
RP SUBUNIT, AND INTERACTION WITH LPTBFG.
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 [8]
RP FUNCTION, AND INTERACTION WITH LPTA.
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 [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH LPTA, AND MUTAGENESIS OF GLY-56;
RP GLY-153 AND 177-LYS--PRO-191.
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 [10]
RP SUBUNIT, AND INTERACTION WITH LPTA.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-191, FUNCTION IN
RP LIPOPOLYSACCHARIDE TRANSPORT, AND SUBCELLULAR LOCATION.
RX PubMed=20720015; DOI=10.1074/jbc.m110.144709;
RA Tran A.X., Dong C., Whitfield C.;
RT "Structure and functional analysis of LptC, a conserved membrane protein
RT involved in the lipopolysaccharide export pathway in Escherichia coli.";
RL J. Biol. Chem. 285:33529-33539(2010).
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. Facilitates the transfer of LPS from the inner membrane
CC to the periplasmic protein LptA. Could be a docking site for LptA.
CC {ECO:0000255|HAMAP-Rule:MF_01915, ECO:0000269|PubMed:16765569,
CC ECO:0000269|PubMed:18424520, ECO:0000269|PubMed:20720015,
CC ECO:0000269|PubMed:21169485, ECO:0000269|PubMed:21195693}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. Interacts with LptA and the LptBFG transporter complex. When
CC overexpressed, can form homodimers in vivo. {ECO:0000255|HAMAP-
CC Rule:MF_01915, ECO:0000269|PubMed:19500581,
CC ECO:0000269|PubMed:20446753, ECO:0000269|PubMed:21169485,
CC ECO:0000269|PubMed:21195693, ECO:0000269|PubMed:22668317}.
CC -!- INTERACTION:
CC P0ADV9; P0ADV1: lptA; NbExp=3; IntAct=EBI-1131969, EBI-1132001;
CC P0ADV9; P0ADV9: lptC; NbExp=4; IntAct=EBI-1131969, EBI-1131969;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01915, ECO:0000269|PubMed:18424520,
CC ECO:0000269|PubMed:20720015}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01915, ECO:0000269|PubMed:18424520,
CC ECO:0000269|PubMed:20720015}.
CC -!- DISRUPTION PHENOTYPE: Leads to irreversible cell damage, growth arrest
CC and an extreme sensitivity to SDS. {ECO:0000269|PubMed:16765569}.
CC -!- MISCELLANEOUS: Interacts with the LptBFG ABC transporter complex, but
CC does not affect its ATPase activity. {ECO:0000305|PubMed:19500581}.
CC -!- SIMILARITY: Belongs to the LptC family. {ECO:0000255|HAMAP-
CC Rule:MF_01915}.
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DR EMBL; U18997; AAA58001.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76231.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77243.1; -; Genomic_DNA.
DR EMBL; U12684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A65111; A65111.
DR RefSeq; NP_417666.1; NC_000913.3.
DR RefSeq; WP_000030537.1; NZ_STEB01000012.1.
DR PDB; 3MY2; X-ray; 2.20 A; A=23-191.
DR PDB; 4B54; X-ray; 2.80 A; A/B=24-191.
DR PDB; 6MI7; EM; 4.20 A; C=1-191.
DR PDBsum; 3MY2; -.
DR PDBsum; 4B54; -.
DR PDBsum; 6MI7; -.
DR AlphaFoldDB; P0ADV9; -.
DR SMR; P0ADV9; -.
DR BioGRID; 4259279; 274.
DR DIP; DIP-12912N; -.
DR IntAct; P0ADV9; 3.
DR MINT; P0ADV9; -.
DR STRING; 511145.b3199; -.
DR jPOST; P0ADV9; -.
DR PaxDb; P0ADV9; -.
DR PRIDE; P0ADV9; -.
DR EnsemblBacteria; AAC76231; AAC76231; b3199.
DR EnsemblBacteria; BAE77243; BAE77243; BAE77243.
DR GeneID; 66672899; -.
DR GeneID; 947722; -.
DR KEGG; ecj:JW3166; -.
DR KEGG; eco:b3199; -.
DR PATRIC; fig|1411691.4.peg.3532; -.
DR EchoBASE; EB2657; -.
DR eggNOG; COG3117; Bacteria.
DR HOGENOM; CLU_105814_2_1_6; -.
DR OMA; YWQVQSK; -.
DR PhylomeDB; P0ADV9; -.
DR BioCyc; EcoCyc:G7664-MON; -.
DR BioCyc; MetaCyc:G7664-MON; -.
DR EvolutionaryTrace; P0ADV9; -.
DR PRO; PR:P0ADV9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; 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; IPI:IntAct.
DR GO; GO:0015221; F:lipopolysaccharide transmembrane transporter activity; 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 DisProt; DP02197; -.
DR HAMAP; MF_01915; LPS_assembly_LptC; 1.
DR InterPro; IPR010664; LipoPS_assembly_LptC-rel.
DR InterPro; IPR026265; LptC.
DR Pfam; PF06835; LptC; 1.
DR PIRSF; PIRSF028513; LptC; 1.
DR TIGRFAMs; TIGR04409; LptC_YrbK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..191
FT /note="Lipopolysaccharide export system protein LptC"
FT /id="PRO_0000169470"
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01915"
FT MUTAGEN 56
FT /note="G->V: Impairs LPS transport. Does not abolish
FT interaction with LptA."
FT /evidence="ECO:0000269|PubMed:21169485"
FT MUTAGEN 153
FT /note="G->R: Impairs LPS transport. Fails to interacts with
FT LptA."
FT /evidence="ECO:0000269|PubMed:21169485"
FT MUTAGEN 177..191
FT /note="Missing: Fails to interact with LptA."
FT /evidence="ECO:0000269|PubMed:21169485"
FT CONFLICT 2
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3MY2"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 107..119
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 125..137
FT /evidence="ECO:0007829|PDB:3MY2"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 142..155
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:3MY2"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:3MY2"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:3MY2"
SQ SEQUENCE 191 AA; 21703 MW; F6BAE79EA232CD95 CRC64;
MSKARRWVII VLSLAVLVMI GINMAEKDDT AQVVVNNNDP TYKSEHTDTL VYNPEGALSY
RLIAQHVEYY SDQAVSWFTQ PVLTTFDKDK IPTWSVKADK AKLTNDRMLY LYGHVEVNAL
VPDSQLRRIT TDNAQINLVT QDVTSEDLVT LYGTTFNSSG LKMRGNLRSK NAELIEKVRT
SYEIQNKQTQ P
