LOLA_ECOLI
ID LOLA_ECOLI Reviewed; 203 AA.
AC P61316; P39178; Q8X5H8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Outer-membrane lipoprotein carrier protein;
DE AltName: Full=P20;
DE Flags: Precursor;
GN Name=lolA; Synonyms=lplA, yzzV; OrderedLocusNames=b0891, JW0874;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 22-39; 45-60;
RP 64-81; 104-115 AND 188-203.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=7628437; DOI=10.1002/j.1460-2075.1995.tb07342.x;
RA Matsuyama S., Tajima T., Tokuda H.;
RT "A novel periplasmic carrier protein involved in the sorting and transport
RT of Escherichia coli lipoproteins destined for the outer membrane.";
RL EMBO J. 14:3365-3372(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 22-33.
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 FUNCTION IN THE REGULATION OF THE RCS SYSTEM.
RX PubMed=11758943; DOI=10.1271/bbb.65.2364;
RA Chen M.H., Takeda S., Yamada H., Ishii Y., Yamashino T., Mizuno T.;
RT "Characterization of the RcsC->YojN->RcsB phosphorelay signaling pathway
RT involved in capsular synthesis in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 65:2364-2367(2001).
RN [7]
RP CHARACTERIZATION OF SORTING SIGNALS.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11592971; DOI=10.1074/jbc.m109307200;
RA Terada M., Kuroda T., Matsuyama S., Tokuda H.;
RT "Lipoprotein sorting signals evaluated as the LolA-dependent release of
RT lipoproteins from the cytoplasmic membrane of Escherichia coli.";
RL J. Biol. Chem. 276:47690-47694(2001).
RN [8]
RP CHARACTERIZATION OF SORTING SIGNALS.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12032293; DOI=10.1073/pnas.112085599;
RA Masuda K., Matsuyama S., Tokuda H.;
RT "Elucidation of the function of lipoprotein-sorting signals that determine
RT membrane localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7390-7395(2002).
RN [9]
RP REQUIREMENT OF AMINOACYLATION FOR RELEASE OF LIPOPROTEINS.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12198129; DOI=10.1074/jbc.m206816200;
RA Fukuda A., Matsuyama S., Hara T., Nakayama J., Nagasawa H., Tokuda H.;
RT "Aminoacylation of the N-terminal cysteine is essential for Lol-dependent
RT release of lipoproteins from membranes but does not depend on lipoprotein
RT sorting signals.";
RL J. Biol. Chem. 277:43512-43518(2002).
RN [10]
RP MUTAGENESIS OF ARG-64.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11587539; DOI=10.1006/bbrc.2001.5705;
RA Miyamoto A., Matsuyama S., Tokuda H.;
RT "Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia
RT coli, defective in the transfer of lipoproteins to LolB.";
RL Biochem. Biophys. Res. Commun. 287:1125-1128(2001).
RN [11]
RP MUTAGENESIS OF PHE-68.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12297303; DOI=10.1016/s0014-5793(02)03305-7;
RA Miyamoto A., Matsuyama S., Tokuda H.;
RT "Dominant negative mutant of a lipoprotein-specific molecular chaperone,
RT LolA, tightly associates with LolCDE.";
RL FEBS Lett. 528:193-196(2002).
RN [12]
RP CRYSTALLIZATION.
RX PubMed=12876347; DOI=10.1107/s090744490301254x;
RA Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., Miki K.;
RT "A practical phasing procedure using the MAD method without the aid of XAFS
RT measurements: successful solution in the structure determination of the
RT outer-membrane lipoprotein carrier LolA.";
RL Acta Crystallogr. D 59:1440-1446(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=12839983; DOI=10.1093/emboj/cdg324;
RA Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., Miki K.;
RT "Crystal structures of bacterial lipoprotein localization factors, LolA and
RT LolB.";
RL EMBO J. 22:3199-3209(2003).
CC -!- FUNCTION: Participates in the translocation of lipoproteins from the
CC inner membrane to the outer membrane. Only forms a complex with a
CC lipoprotein if the residue after the N-terminal Cys is not an aspartate
CC (The Asp acts as a targeting signal to indicate that the lipoprotein
CC should stay in the inner membrane); the inner membrane retention signal
CC functions at the release step. {ECO:0000269|PubMed:11758943}.
CC -!- FUNCTION: May act as a regulator of the RCS-phosphorelay signal
CC transduction pathway. {ECO:0000269|PubMed:11758943}.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P61316; P61320: lolB; NbExp=2; IntAct=EBI-553532, EBI-1122794;
CC P61316; P0ADC3: lolC; NbExp=4; IntAct=EBI-553532, EBI-15765497;
CC P61316; P0A912: pal; NbExp=2; IntAct=EBI-553532, EBI-1124760;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the LolA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08390.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA35616.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D49398; BAA08390.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73977.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35616.1; ALT_INIT; Genomic_DNA.
DR PIR; S57828; S57828.
DR RefSeq; NP_415411.2; NC_000913.3.
DR RefSeq; WP_001295343.1; NZ_STEB01000006.1.
DR PDB; 1IWL; X-ray; 1.65 A; A=22-203.
DR PDB; 1UA8; X-ray; 1.90 A; A=22-203.
DR PDB; 2ZPC; X-ray; 2.35 A; A=22-203.
DR PDB; 2ZPD; X-ray; 1.85 A; A=22-203.
DR PDB; 3KSN; X-ray; 1.65 A; A=22-203.
DR PDB; 6F3Z; X-ray; 2.00 A; B/D=22-203.
DR PDB; 6FHM; X-ray; 2.39 A; A/B=22-203.
DR PDB; 7ARM; EM; 3.60 A; A=20-203.
DR PDBsum; 1IWL; -.
DR PDBsum; 1UA8; -.
DR PDBsum; 2ZPC; -.
DR PDBsum; 2ZPD; -.
DR PDBsum; 3KSN; -.
DR PDBsum; 6F3Z; -.
DR PDBsum; 6FHM; -.
DR PDBsum; 7ARM; -.
DR AlphaFoldDB; P61316; -.
DR SMR; P61316; -.
DR BioGRID; 4260649; 338.
DR DIP; DIP-35675N; -.
DR IntAct; P61316; 16.
DR MINT; P61316; -.
DR STRING; 511145.b0891; -.
DR BindingDB; P61316; -.
DR ChEMBL; CHEMBL3309024; -.
DR TCDB; 1.B.46.1.1; the outer membrane lolab lipoprotein insertion apparatus (lolab) family.
DR SWISS-2DPAGE; P61316; -.
DR jPOST; P61316; -.
DR PaxDb; P61316; -.
DR PRIDE; P61316; -.
DR EnsemblBacteria; AAC73977; AAC73977; b0891.
DR EnsemblBacteria; BAA35616; BAA35616; BAA35616.
DR GeneID; 66670835; -.
DR GeneID; 948989; -.
DR KEGG; ecj:JW0874; -.
DR KEGG; eco:b0891; -.
DR PATRIC; fig|1411691.4.peg.1386; -.
DR EchoBASE; EB2548; -.
DR eggNOG; COG2834; Bacteria.
DR HOGENOM; CLU_087560_1_1_6; -.
DR InParanoid; P61316; -.
DR OMA; YDPFVEQ; -.
DR PhylomeDB; P61316; -.
DR BioCyc; EcoCyc:G6465-MON; -.
DR BioCyc; MetaCyc:G6465-MON; -.
DR EvolutionaryTrace; P61316; -.
DR PRO; PR:P61316; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0044874; P:lipoprotein localization to outer membrane; IDA:CACAO.
DR GO; GO:0042953; P:lipoprotein transport; IDA:EcoCyc.
DR CDD; cd16325; LolA; 1.
DR HAMAP; MF_00240; LolA; 1.
DR InterPro; IPR029046; LolA/LolB/LppX.
DR InterPro; IPR004564; OM_lipoprot_carrier_LolA-like.
DR InterPro; IPR018323; OM_lipoprot_carrier_LolA_Pbac.
DR PANTHER; PTHR35869; PTHR35869; 1.
DR Pfam; PF03548; LolA; 1.
DR SUPFAM; SSF89392; SSF89392; 1.
DR TIGRFAMs; TIGR00547; lolA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Periplasm;
KW Protein transport; Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7628437,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 22..203
FT /note="Outer-membrane lipoprotein carrier protein"
FT /id="PRO_0000018256"
FT MUTAGEN 64
FT /note="R->L: Loss of ability to transfer lipoproteins to
FT LolB."
FT /evidence="ECO:0000269|PubMed:11587539"
FT MUTAGEN 68
FT /note="F->E: Loss of ability to bind lipoproteins."
FT /evidence="ECO:0000269|PubMed:12297303"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 35..46
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2ZPC"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:1IWL"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 78..91
FT /evidence="ECO:0007829|PDB:1IWL"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1IWL"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1IWL"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3KSN"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:1IWL"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 170..181
FT /evidence="ECO:0007829|PDB:1IWL"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1IWL"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1IWL"
SQ SEQUENCE 203 AA; 22497 MW; F2884D82D8DFEF1D CRC64;
MKKIAITCAL LSSLVASSVW ADAASDLKSR LDKVSSFHAS FTQKVTDGSG AAVQEGQGDL
WVKRPNLFNW HMTQPDESIL VSDGKTLWFY NPFVEQATAT WLKDATGNTP FMLIARNQSS
DWQQYNIKQN GDDFVLTPKA SNGNLKQFTI NVGRDGTIHQ FSAVEQDDQR SSYQLKSQQN
GAVDAAKFTF TPPQGVTVDD QRK
