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Protein

Outer membrane lipoprotein RcsF

Gene

rcsF

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

Functioni

Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.UniRule annotation4 Publications

GO - Biological processi

  • colanic acid biosynthetic process Source: EcoCyc
  • intracellular signal transduction Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Capsule biogenesis/degradation

Enzyme and pathway databases

BioCyciEcoCyc:RCSF-MONOMER.
ECOL316407:JW0192-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Outer membrane lipoprotein RcsFUniRule annotation
Gene namesi
Name:rcsF1 PublicationUniRule annotation
Ordered Locus Names:b0196, JW0192
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11502. rcsF.

Subcellular locationi

GO - Cellular componenti

  • anchored component of periplasmic side of cell outer membrane Source: UniProtKB-HAMAP
  • cell outer membrane Source: EcoCyc
  • external side of cell outer membrane Source: EcoCyc
  • intracellular Source: GOC
  • periplasmic side of cell outer membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71C → S: Does not affect exopolysaccharide biosynthesis. 1 Publication
Mutagenesisi16 – 161C → S: Strongly decreases exopolysaccharide biosynthesis. 1 Publication
Mutagenesisi74 – 741C → S: Mucoid phenotype. Decreases exopolysaccharide biosynthesis. 2 Publications
Mutagenesisi89 – 891R → A: Does not affect exopolysaccharide biosynthesis; when associated with A-90. 1 Publication
Mutagenesisi90 – 901K → A: Does not affect exopolysaccharide biosynthesis; when associated with A-89. 1 Publication
Mutagenesisi109 – 1091C → S: Does not activate the production of capsule polysaccharides. 2 Publications
Mutagenesisi118 – 1181C → S: Mucoid phenotype. Decreases exopolysaccharide biosynthesis. 2 Publications
Mutagenesisi124 – 1241C → S: Does not activate the production of capsule polysaccharides. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515UniRule annotationAdd
BLAST
Chaini16 – 134119Outer membrane lipoprotein RcsFPRO_0000097208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi16 – 161N-palmitoyl cysteineUniRule annotation
Lipidationi16 – 161S-diacylglycerol cysteineUniRule annotation
Disulfide bondi74 ↔ 118UniRule annotation2 Publications
Disulfide bondi109 ↔ 124UniRule annotation2 Publications

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Proteomic databases

EPDiP69411.
PaxDbiP69411.

Interactioni

Subunit structurei

Interacts with DsbC.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
bamAP0A9403EBI-1114706,EBI-907371
ompAP0A9103EBI-1114706,EBI-371347

Protein-protein interaction databases

BioGridi4259530. 9 interactions.
IntActiP69411. 10 interactions.
STRINGi511145.b0196.

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 523Combined sources
Helixi55 – 584Combined sources
Beta strandi63 – 7513Combined sources
Helixi85 – 9814Combined sources
Beta strandi102 – 11312Combined sources
Beta strandi119 – 13113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L8YNMR-A31-134[»]
2Y1BX-ray2.00A17-134[»]
ProteinModelPortaliP69411.
SMRiP69411. Positions 31-134.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 5019PRRAdd
BLAST

Domaini

Contains an N-terminal proline-rich region (PRR), which probably plays an important role in the regulation of function of RcsF and activation of the Rcs signaling system.1 Publication

Sequence similaritiesi

Belongs to the RcsF family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108R8X. Bacteria.
ENOG4111FP8. LUCA.
HOGENOMiHOG000280809.
InParanoidiP69411.
KOiK06080.
OMAiFRDMGEV.

Family and domain databases

HAMAPiMF_00976. RcsF. 1 hit.
InterProiIPR030852. RcsF.
[Graphical view]
PfamiPF16358. RcsF. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P69411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALPICLVA LMLSGCSMLS RSPVEPVQST APQPKAEPAK PKAPRATPVR
60 70 80 90 100
IYTNAEELVG KPFRDLGEVS GDSCQASNQD SPPSIPTARK RMQINASKMK
110 120 130
ANAVLLHSCE VTSGTPGCYR QAVCIGSALN ITAK
Length:134
Mass (Da):14,163
Last modified:March 1, 2005 - v1
Checksum:i824F82151C07BB41
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 382EP → DA in AAA24508 (PubMed:1459951).Curated
Sequence conflicti46 – 461Missing in AAA24508 (PubMed:1459951).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04474 Genomic DNA. Translation: AAA24508.1.
D15061 Genomic DNA. Translation: BAA03656.1.
U70214 Genomic DNA. Translation: AAB08624.1.
U00096 Genomic DNA. Translation: AAC73307.1.
AP009048 Genomic DNA. Translation: BAA77873.2.
PIRiD64744.
RefSeqiNP_414738.1. NC_000913.3.
WP_001202329.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73307; AAC73307; b0196.
BAA77873; BAA77873; BAA77873.
GeneIDi949113.
KEGGiecj:JW0192.
eco:b0196.
PATRICi32115505. VBIEscCol129921_0204.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04474 Genomic DNA. Translation: AAA24508.1.
D15061 Genomic DNA. Translation: BAA03656.1.
U70214 Genomic DNA. Translation: AAB08624.1.
U00096 Genomic DNA. Translation: AAC73307.1.
AP009048 Genomic DNA. Translation: BAA77873.2.
PIRiD64744.
RefSeqiNP_414738.1. NC_000913.3.
WP_001202329.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L8YNMR-A31-134[»]
2Y1BX-ray2.00A17-134[»]
ProteinModelPortaliP69411.
SMRiP69411. Positions 31-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259530. 9 interactions.
IntActiP69411. 10 interactions.
STRINGi511145.b0196.

Proteomic databases

EPDiP69411.
PaxDbiP69411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73307; AAC73307; b0196.
BAA77873; BAA77873; BAA77873.
GeneIDi949113.
KEGGiecj:JW0192.
eco:b0196.
PATRICi32115505. VBIEscCol129921_0204.

Organism-specific databases

EchoBASEiEB1465.
EcoGeneiEG11502. rcsF.

Phylogenomic databases

eggNOGiENOG4108R8X. Bacteria.
ENOG4111FP8. LUCA.
HOGENOMiHOG000280809.
InParanoidiP69411.
KOiK06080.
OMAiFRDMGEV.

Enzyme and pathway databases

BioCyciEcoCyc:RCSF-MONOMER.
ECOL316407:JW0192-MONOMER.

Miscellaneous databases

PROiP69411.

Family and domain databases

HAMAPiMF_00976. RcsF. 1 hit.
InterProiIPR030852. RcsF.
[Graphical view]
PfamiPF16358. RcsF. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRCSF_ECOLI
AccessioniPrimary (citable) accession number: P69411
Secondary accession number(s): P28633
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: September 7, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The formation of the non-consecutive disulfides depends on the periplasmic disulfide isomerase DsbC. The disulfide bond between Cys-109 and Cys-124 is particularly important for the assembly of an active RcsF (PubMed:21454485).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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.