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Protein

Modulator of FtsH protease YccA

Gene

yccA

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

Functioni

Negatively modulates the activity of the FtsH protease for membrane substrates. Overexpression or stabilizing YccA counteracts the FtsH-mediated degradation of SecY when the SecYEG preprotein translocator is jammed.1 Publication

GO - Biological processi

  • negative regulation of apoptotic process Source: InterPro
  • regulation of proteolysis Source: EcoCyc
Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:EG11113-MONOMER.
ECOL316407:JW0953-MONOMER.

Protein family/group databases

TCDBi1.A.14.2.1. the testis-enhanced gene transfer (tegt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Modulator of FtsH protease YccA
Gene namesi
Name:yccA
Ordered Locus Names:b0970, JW0953
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11113. yccA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicCuratedAdd
BLAST
Transmembranei23 – 4321HelicalSequence analysisAdd
BLAST
Topological domaini44 – 463ExtracellularCurated
Transmembranei47 – 6418HelicalSequence analysisAdd
BLAST
Topological domaini65 – 739CytoplasmicCurated
Transmembranei74 – 9421HelicalSequence analysisAdd
BLAST
Topological domaini95 – 10410ExtracellularCurated
Transmembranei105 – 12521HelicalSequence analysisAdd
BLAST
Topological domaini126 – 1327CytoplasmicCurated
Transmembranei133 – 15321HelicalSequence analysisAdd
BLAST
Topological domaini154 – 1574ExtracellularCurated
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Topological domaini179 – 19517CytoplasmicCuratedAdd
BLAST
Transmembranei196 – 21621HelicalSequence analysisAdd
BLAST
Topological domaini217 – 2193Extracellular

GO - Cellular componenti

  • integral component of membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No effect on SecY degradation.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 1212MDRIV…SHDRT → MTMITPSLHDRI: Protein is as sensitive to FtsH degradation as the wild-type. 1 PublicationAdd
BLAST
Mutagenesisi5 – 128Missing in yccA11; increases the half-life of overexpressed SecY, F(0) ATP synthase subunit a and itself in an HflKC-dependent fashion, but has no effect on degradation of cytosolic substrates sigma-32 or the phage lambda cII protein. Partially dominant over the wild-type allele. This protein interacts with but is not degraded by FtsH. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219Modulator of FtsH protease YccAPRO_0000179102Add
BLAST

Post-translational modificationi

YccA is processively degraded by FtsH; degradation initiates via the approximately 20 residue N-terminal tail in a sequence non-specific manner. The deletion mutant yccA11 is resistant to FtsH-mediated degradation, probably because it is too short to be degraded by FtsH.

Proteomic databases

PaxDbiP0AAC6.
PRIDEiP0AAC6.

Expressioni

Inductioni

Regulated in a Cpx-dependent fashion.1 Publication

Interactioni

Subunit structurei

Both wild-type and the yccA11 mutant interact with the FtsH/HflKC complex.

Protein-protein interaction databases

BioGridi4260037. 11 interactions.
DIPiDIP-47918N.
IntActiP0AAC6. 1 interaction.
MINTiMINT-1274885.
STRINGi511145.b0970.

Structurei

3D structure databases

ProteinModelPortaliP0AAC6.
SMRiP0AAC6. Positions 15-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the BI1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108MN8. Bacteria.
COG0670. LUCA.
HOGENOMiHOG000060391.
InParanoidiP0AAC6.
KOiK19416.
OMAiMGDVIGM.
OrthoDBiEOG6PZXBH.
PhylomeDBiP0AAC6.

Family and domain databases

InterProiIPR006213. Bax_inhbtr1_CS.
IPR006214. Bax_inhibitor_1-related.
[Graphical view]
PANTHERiPTHR23291. PTHR23291. 1 hit.
PROSITEiPS01243. BI1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AAC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRIVSSSHD RTSLLSTHKV LRNTYFLLSL TLAFSAITAT ASTVLMLPSP
60 70 80 90 100
GLILTLVGMY GLMFLTYKTA NKPTGIISAF AFTGFLGYIL GPILNTYLSA
110 120 130 140 150
GMGDVIAMAL GGTALVFFCC SAYVLTTRKD MSFLGGMLMA GIVVVLIGMV
160 170 180 190 200
ANIFLQLPAL HLAISAVFIL ISSGAILFET SNIIHGGETN YIRATVSLYV
210
SLYNIFVSLL SILGFASRD
Length:219
Mass (Da):23,363
Last modified:April 1, 1988 - v1
Checksum:i4F787B853042ACD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00547 Genomic DNA. Translation: CAA25218.1.
U00096 Genomic DNA. Translation: AAC74056.1.
AP009048 Genomic DNA. Translation: BAA35735.1.
PIRiS07180.
RefSeqiNP_415490.1. NC_000913.3.
WP_000375136.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74056; AAC74056; b0970.
BAA35735; BAA35735; BAA35735.
GeneIDi946016.
KEGGiecj:JW0953.
eco:b0970.
PATRICi32117161. VBIEscCol129921_1005.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00547 Genomic DNA. Translation: CAA25218.1.
U00096 Genomic DNA. Translation: AAC74056.1.
AP009048 Genomic DNA. Translation: BAA35735.1.
PIRiS07180.
RefSeqiNP_415490.1. NC_000913.3.
WP_000375136.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AAC6.
SMRiP0AAC6. Positions 15-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260037. 11 interactions.
DIPiDIP-47918N.
IntActiP0AAC6. 1 interaction.
MINTiMINT-1274885.
STRINGi511145.b0970.

Protein family/group databases

TCDBi1.A.14.2.1. the testis-enhanced gene transfer (tegt) family.

Proteomic databases

PaxDbiP0AAC6.
PRIDEiP0AAC6.

Protocols and materials databases

DNASUi946016.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74056; AAC74056; b0970.
BAA35735; BAA35735; BAA35735.
GeneIDi946016.
KEGGiecj:JW0953.
eco:b0970.
PATRICi32117161. VBIEscCol129921_1005.

Organism-specific databases

EchoBASEiEB1104.
EcoGeneiEG11113. yccA.

Phylogenomic databases

eggNOGiENOG4108MN8. Bacteria.
COG0670. LUCA.
HOGENOMiHOG000060391.
InParanoidiP0AAC6.
KOiK19416.
OMAiMGDVIGM.
OrthoDBiEOG6PZXBH.
PhylomeDBiP0AAC6.

Enzyme and pathway databases

BioCyciEcoCyc:EG11113-MONOMER.
ECOL316407:JW0953-MONOMER.

Miscellaneous databases

PROiP0AAC6.

Family and domain databases

InterProiIPR006213. Bax_inhbtr1_CS.
IPR006214. Bax_inhibitor_1-related.
[Graphical view]
PANTHERiPTHR23291. PTHR23291. 1 hit.
PROSITEiPS01243. BI1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The E. coli divE mutation, which differentially inhibits synthesis of certain proteins, is in tRNASer1."
    Tamura F., Nishimura S., Ohki M.
    EMBO J. 3:1103-1107(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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. "Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: an implication from the interference by a mutant form of a new substrate protein, YccA."
    Kihara A., Akiyama Y., Ito K.
    J. Mol. Biol. 279:175-188(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE FOR FTSH, INTERACTION WITH FTSH AND HFLKC, MUTAGENESIS OF 5-VAL--THR-12, DISRUPTION PHENOTYPE.
    Strain: K12 / CSH26 / AD16.
  6. "Dislocation of membrane proteins in FtsH-mediated proteolysis."
    Kihara A., Akiyama Y., Ito K.
    EMBO J. 18:2970-2981(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY, MUTAGENESIS OF 1-MET--THR-12.
    Strain: K12 / CSH26 / AD16.
  7. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY."
    van Stelten J., Silva F., Belin D., Silhavy T.J.
    Science 325:753-756(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MODULATING FTSH ACTIVITY, INDUCTION.
    Strain: K12 / MC4100.
  9. "Quality control of cytoplasmic membrane proteins in Escherichia coli."
    Akiyama Y.
    J. Biochem. 146:449-454(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiYCCA_ECOLI
AccessioniPrimary (citable) accession number: P0AAC6
Secondary accession number(s): P06967
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 11, 2016
This is version 89 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

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.