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Protein

Outer-membrane lipoprotein carrier protein

Gene

lolA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step.1 Publication
May act as a regulator of the RCS-phosphorelay signal transduction pathway.1 Publication

GO - Molecular functioni

  • lipoprotein transporter activity Source: EcoCyc

GO - Biological processi

  • chaperone-mediated protein transport across periplasmic space Source: CACAO
  • lipoprotein localization to outer membrane Source: CACAO
  • lipoprotein transport Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:G6465-MONOMER.
ECOL316407:JW0874-MONOMER.

Protein family/group databases

TCDBi1.B.46.1.1. the outer membrane lolab lipoprotein insertion apparatus (lolab) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Outer-membrane lipoprotein carrier protein
Alternative name(s):
P20
Gene namesi
Name:lolA
Synonyms:lplA, yzzV
Ordered Locus Names:b0891, JW0874
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12684. lolA.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641R → L: Loss of ability to transfer lipoproteins to LolB. 1 Publication
Mutagenesisi68 – 681F → E: Loss of ability to bind lipoproteins. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21212 PublicationsAdd
BLAST
Chaini22 – 203182Outer-membrane lipoprotein carrier proteinPRO_0000018256Add
BLAST

Proteomic databases

EPDiP61316.
PaxDbiP61316.
PRIDEiP61316.

2D gel databases

SWISS-2DPAGEP61316.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
lppP697761EBI-553532,EBI-909750

Protein-protein interaction databases

BioGridi4260649. 271 interactions.
DIPiDIP-35675N.
IntActiP61316. 11 interactions.
MINTiMINT-1249033.
STRINGi511145.b0891.

Structurei

Secondary structure

1
203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 308Combined sources
Beta strandi35 – 4612Combined sources
Beta strandi48 – 514Combined sources
Beta strandi54 – 6310Combined sources
Turni64 – 663Combined sources
Beta strandi67 – 726Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 9114Combined sources
Helixi92 – 943Combined sources
Beta strandi96 – 1016Combined sources
Helixi102 – 1043Combined sources
Turni105 – 1073Combined sources
Helixi110 – 1167Combined sources
Helixi119 – 1224Combined sources
Beta strandi125 – 1306Combined sources
Beta strandi133 – 14210Combined sources
Beta strandi144 – 1529Combined sources
Beta strandi158 – 1658Combined sources
Beta strandi170 – 18112Combined sources
Helixi185 – 1884Combined sources
Beta strandi197 – 2004Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWLX-ray1.65A22-203[»]
1UA8X-ray1.90A22-203[»]
2ZPCX-ray2.35A22-203[»]
2ZPDX-ray1.85A22-203[»]
3KSNX-ray1.65A22-203[»]
ProteinModelPortaliP61316.
SMRiP61316. Positions 22-203.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61316.

Family & Domainsi

Sequence similaritiesi

Belongs to the LolA family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107Y7W. Bacteria.
COG2834. LUCA.
HOGENOMiHOG000257501.
InParanoidiP61316.
KOiK03634.
OMAiYDPFVEQ.
OrthoDBiEOG6677VP.
PhylomeDBiP61316.

Family and domain databases

HAMAPiMF_00240. LolA.
InterProiIPR029046. LolA/LolB/LppX.
IPR004564. OM_lipoprot_carrier_LolA-like.
IPR018323. OM_lipoprot_carrier_LolA_Pbac.
[Graphical view]
PfamiPF03548. LolA. 1 hit.
[Graphical view]
SUPFAMiSSF89392. SSF89392. 1 hit.
TIGRFAMsiTIGR00547. lolA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61316-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIAITCAL LSSLVASSVW ADAASDLKSR LDKVSSFHAS FTQKVTDGSG
60 70 80 90 100
AAVQEGQGDL WVKRPNLFNW HMTQPDESIL VSDGKTLWFY NPFVEQATAT
110 120 130 140 150
WLKDATGNTP FMLIARNQSS DWQQYNIKQN GDDFVLTPKA SNGNLKQFTI
160 170 180 190 200
NVGRDGTIHQ FSAVEQDDQR SSYQLKSQQN GAVDAAKFTF TPPQGVTVDD

QRK
Length:203
Mass (Da):22,497
Last modified:May 10, 2004 - v1
Checksum:iF2884D82D8DFEF1D
GO

Sequence cautioni

The sequence BAA08390.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA35616.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49398 Genomic DNA. Translation: BAA08390.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73977.2.
AP009048 Genomic DNA. Translation: BAA35616.1. Different initiation.
PIRiS57828.
RefSeqiNP_415411.2. NC_000913.3.
WP_001295343.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73977; AAC73977; b0891.
BAA35616; BAA35616; BAA35616.
GeneIDi948989.
KEGGiecj:JW0874.
eco:b0891.
PATRICi32116993. VBIEscCol129921_0921.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49398 Genomic DNA. Translation: BAA08390.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73977.2.
AP009048 Genomic DNA. Translation: BAA35616.1. Different initiation.
PIRiS57828.
RefSeqiNP_415411.2. NC_000913.3.
WP_001295343.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWLX-ray1.65A22-203[»]
1UA8X-ray1.90A22-203[»]
2ZPCX-ray2.35A22-203[»]
2ZPDX-ray1.85A22-203[»]
3KSNX-ray1.65A22-203[»]
ProteinModelPortaliP61316.
SMRiP61316. Positions 22-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260649. 271 interactions.
DIPiDIP-35675N.
IntActiP61316. 11 interactions.
MINTiMINT-1249033.
STRINGi511145.b0891.

Protein family/group databases

TCDBi1.B.46.1.1. the outer membrane lolab lipoprotein insertion apparatus (lolab) family.

2D gel databases

SWISS-2DPAGEP61316.

Proteomic databases

EPDiP61316.
PaxDbiP61316.
PRIDEiP61316.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73977; AAC73977; b0891.
BAA35616; BAA35616; BAA35616.
GeneIDi948989.
KEGGiecj:JW0874.
eco:b0891.
PATRICi32116993. VBIEscCol129921_0921.

Organism-specific databases

EchoBASEiEB2548.
EcoGeneiEG12684. lolA.

Phylogenomic databases

eggNOGiENOG4107Y7W. Bacteria.
COG2834. LUCA.
HOGENOMiHOG000257501.
InParanoidiP61316.
KOiK03634.
OMAiYDPFVEQ.
OrthoDBiEOG6677VP.
PhylomeDBiP61316.

Enzyme and pathway databases

BioCyciEcoCyc:G6465-MONOMER.
ECOL316407:JW0874-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP61316.
PROiP61316.

Family and domain databases

HAMAPiMF_00240. LolA.
InterProiIPR029046. LolA/LolB/LppX.
IPR004564. OM_lipoprot_carrier_LolA-like.
IPR018323. OM_lipoprot_carrier_LolA_Pbac.
[Graphical view]
PfamiPF03548. LolA. 1 hit.
[Graphical view]
SUPFAMiSSF89392. SSF89392. 1 hit.
TIGRFAMsiTIGR00547. lolA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane."
    Matsuyama S., Tajima T., Tokuda H.
    EMBO J. 14:3365-3372(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-39; 45-60; 64-81; 104-115 AND 188-203.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-33.
    Strain: K12 / EMG2.
  6. "Characterization of the RcsC->YojN->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli."
    Chen M.H., Takeda S., Yamada H., Ishii Y., Yamashino T., Mizuno T.
    Biosci. Biotechnol. Biochem. 65:2364-2367(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE REGULATION OF THE RCS SYSTEM.
  7. "Lipoprotein sorting signals evaluated as the LolA-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli."
    Terada M., Kuroda T., Matsuyama S., Tokuda H.
    J. Biol. Chem. 276:47690-47694(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF SORTING SIGNALS.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  8. "Elucidation of the function of lipoprotein-sorting signals that determine membrane localization."
    Masuda K., Matsuyama S., Tokuda H.
    Proc. Natl. Acad. Sci. U.S.A. 99:7390-7395(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF SORTING SIGNALS.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  9. "Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals."
    Fukuda A., Matsuyama S., Hara T., Nakayama J., Nagasawa H., Tokuda H.
    J. Biol. Chem. 277:43512-43518(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REQUIREMENT OF AMINOACYLATION FOR RELEASE OF LIPOPROTEINS.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  10. "Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB."
    Miyamoto A., Matsuyama S., Tokuda H.
    Biochem. Biophys. Res. Commun. 287:1125-1128(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-64.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  11. "Dominant negative mutant of a lipoprotein-specific molecular chaperone, LolA, tightly associates with LolCDE."
    Miyamoto A., Matsuyama S., Tokuda H.
    FEBS Lett. 528:193-196(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-68.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  12. "A practical phasing procedure using the MAD method without the aid of XAFS measurements: successful solution in the structure determination of the outer-membrane lipoprotein carrier LolA."
    Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., Miki K.
    Acta Crystallogr. D 59:1440-1446(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  13. "Crystal structures of bacterial lipoprotein localization factors, LolA and LolB."
    Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., Miki K.
    EMBO J. 22:3199-3209(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Entry informationi

Entry nameiLOLA_ECOLI
AccessioniPrimary (citable) accession number: P61316
Secondary accession number(s): P39178, Q8X5H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: March 16, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.