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Protein

Outer-membrane lipoprotein LolB

Gene

lolB

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

Functioni

Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability.

GO - Molecular functioni

  • lipopeptide binding Source: EcoCyc
  • protein transporter activity Source: UniProtKB-HAMAP

GO - Biological processi

  • lipid localization Source: EcoCyc
  • lipoprotein localization to outer membrane Source: CACAO
  • lipoprotein metabolic process Source: EcoCyc
  • localization within membrane Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11293-MONOMER.
ECOL316407:JW1200-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 LolB
Gene namesi
Name:lolB
Synonyms:hemM, ychC
Ordered Locus Names:b1209, JW1200
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11293. lolB.

Subcellular locationi

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 207186Outer-membrane lipoprotein LolBPRO_0000018296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi22 – 221N-palmitoyl cysteine1 Publication
Lipidationi22 – 221S-diacylglycerol cysteine1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP61320.
PRIDEiP61320.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

DIPiDIP-35933N.
IntActiP61320. 7 interactions.
MINTiMINT-7259909.
STRINGi511145.b1209.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 363Combined sources
Helixi37 – 4711Combined sources
Beta strandi51 – 6111Combined sources
Beta strandi66 – 7611Combined sources
Turni77 – 793Combined sources
Beta strandi80 – 867Combined sources
Beta strandi92 – 998Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi112 – 1165Combined sources
Helixi118 – 1269Combined sources
Helixi132 – 1387Combined sources
Turni139 – 1413Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi157 – 16610Combined sources
Beta strandi168 – 1736Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi187 – 1915Combined sources
Beta strandi196 – 20712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWMX-ray1.90A/B22-207[»]
1IWNX-ray2.20A22-207[»]
ProteinModelPortaliP61320.
SMRiP61320. Positions 31-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61320.

Family & Domainsi

Sequence similaritiesi

Belongs to the LolB family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3017.
HOGENOMiHOG000119778.
InParanoidiP61320.
KOiK02494.
OMAiYQTRGSF.
OrthoDBiEOG6R5C6M.

Family and domain databases

HAMAPiMF_00233. LolB.
InterProiIPR029046. LolA/LolB/LppX.
IPR004565. OM_lipoprot_LolB.
[Graphical view]
PfamiPF03550. LolB. 1 hit.
[Graphical view]
SUPFAMiSSF89392. SSF89392. 1 hit.
TIGRFAMsiTIGR00548. lolB. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61320-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLPDFRLIR LLPLAALVLT ACSVTTPKGP GKSPDSPQWR QHQQDVRNLN
60 70 80 90 100
QYQTRGAFAY ISDQQKVYAR FFWQQTGQDR YRLLLTNPLG STELELNAQP
110 120 130 140 150
GNVQLVDNKG QRYTADDAEE MIGKLTGMPI PLNSLRQWIL GLPGDATDYK
160 170 180 190 200
LDDQYRLSEI TYSQNGKNWK VVYGGYDTKT QPAMPANMEL TDGGQRIKLK

MDNWIVK
Length:207
Mass (Da):23,551
Last modified:May 10, 2004 - v1
Checksum:iC517F6E7353B8551
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121L → V in BAA01105 (PubMed:1427085).Curated
Sequence conflicti41 – 422QH → HD in AAC43435 (PubMed:7543480).Curated
Sequence conflicti176 – 20732YDTKT…NWIVK → MTPKRNLRCQPIWNSPTVVN ASS in AAC43435 (PubMed:7543480).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77237 Genomic DNA. Translation: AAA24433.1.
D10264 Genomic DNA. Translation: BAA01105.1.
U18555 Genomic DNA. Translation: AAC43435.1.
U00096 Genomic DNA. Translation: AAC74293.1.
AP009048 Genomic DNA. Translation: BAA36067.1.
PIRiA47706.
RefSeqiNP_415727.1. NC_000913.3.
WP_001130692.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC74293; AAC74293; b1209.
BAA36067; BAA36067; BAA36067.
GeneIDi945775.
KEGGieco:b1209.
PATRICi32117670. VBIEscCol129921_1257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77237 Genomic DNA. Translation: AAA24433.1.
D10264 Genomic DNA. Translation: BAA01105.1.
U18555 Genomic DNA. Translation: AAC43435.1.
U00096 Genomic DNA. Translation: AAC74293.1.
AP009048 Genomic DNA. Translation: BAA36067.1.
PIRiA47706.
RefSeqiNP_415727.1. NC_000913.3.
WP_001130692.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWMX-ray1.90A/B22-207[»]
1IWNX-ray2.20A22-207[»]
ProteinModelPortaliP61320.
SMRiP61320. Positions 31-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35933N.
IntActiP61320. 7 interactions.
MINTiMINT-7259909.
STRINGi511145.b1209.

Protein family/group databases

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

Proteomic databases

PaxDbiP61320.
PRIDEiP61320.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74293; AAC74293; b1209.
BAA36067; BAA36067; BAA36067.
GeneIDi945775.
KEGGieco:b1209.
PATRICi32117670. VBIEscCol129921_1257.

Organism-specific databases

EchoBASEiEB1270.
EcoGeneiEG11293. lolB.

Phylogenomic databases

eggNOGiCOG3017.
HOGENOMiHOG000119778.
InParanoidiP61320.
KOiK02494.
OMAiYQTRGSF.
OrthoDBiEOG6R5C6M.

Enzyme and pathway databases

BioCyciEcoCyc:EG11293-MONOMER.
ECOL316407:JW1200-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP61320.
PROiP61320.

Family and domain databases

HAMAPiMF_00233. LolB.
InterProiIPR029046. LolA/LolB/LppX.
IPR004565. OM_lipoprot_LolB.
[Graphical view]
PfamiPF03550. LolB. 1 hit.
[Graphical view]
SUPFAMiSSF89392. SSF89392. 1 hit.
TIGRFAMsiTIGR00548. lolB. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of genes involved in the biosynthesis of delta-aminolevulinic acid in Escherichia coli."
    Ikemi M., Murakami K., Hashimoto M., Murooka Y.
    Gene 121:127-132(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Characterization of the hemA-prs region of the Escherichia coli and Salmonella typhimurium chromosomes: identification of two open reading frames and implications for prs expression."
    Post D.A., Hove-Jensen B., Switzer R.L.
    J. Gen. Microbiol. 139:259-266(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12."
    Strohmaier H., Remler P., Renner W., Hoegenauer G.
    J. Bacteriol. 177:4488-4500(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "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.
  7. "A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli."
    Matsuyama S., Yokota N., Tokuda H.
    EMBO J. 16:6947-6955(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, DIACYLGLYCEROL AT CYS-22, PALMITOYLATION AT CYS-22, PARTIAL PROTEIN SEQUENCE.
  8. "Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for Escherichia coli and causes accumulation of lipoprotein localization intermediates in the periplasm."
    Tanaka K., Matsuyama S., Tokuda H.
    J. Bacteriol. 183:6538-6542(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMPORTANCE FOR VIABILITY.
    Strain: K12.
  9. "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 (1.9 ANGSTROMS).

Entry informationi

Entry nameiLOLB_ECOLI
AccessioniPrimary (citable) accession number: P61320
Secondary accession number(s): P24208, Q46753
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 22, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be involved in delta-aminolevulinic acid biosynthesis.1 Publication

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

External Data

Dasty 3

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 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.