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P0ABC7

- HFLK_ECOLI

UniProt

P0ABC7 - HFLK_ECOLI

Protein

Modulator of FtsH protease HflK

Gene

hflK

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (08 Nov 2005)
      Previous versions | rss
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    Functioni

    HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins.1 Publication

    GO - Molecular functioni

    1. protein binding Source: EcoCyc

    GO - Biological processi

    1. negative regulation of metalloenzyme activity Source: EcoCyc
    2. response to heat Source: EcoliWiki

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10436-MONOMER.
    ECOL316407:JW4132-MONOMER.
    MetaCyc:EG10436-MONOMER.

    Protein family/group databases

    MEROPSiI87.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modulator of FtsH protease HflK
    Gene namesi
    Name:hflK
    Synonyms:hflA
    Ordered Locus Names:b4174, JW4132
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10436. hflK.

    Subcellular locationi

    Cell inner membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of external side of plasma membrane Source: EcoCyc

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi145 – 1451A → V in hflK13; stabilizes overproduced SecY but not overproduced cII protein. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419Modulator of FtsH protease HflKPRO_0000094085Add
    BLAST

    Proteomic databases

    PaxDbiP0ABC7.
    PRIDEiP0ABC7.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ABC7.

    Interactioni

    Subunit structurei

    HflC and HflK interact to form a complex, originally called HflA, now called HflKC. HflKC interacts with FtsH; complex formation is stimulated by ATP, and with YccA.3 Publications

    Protein-protein interaction databases

    DIPiDIP-47481N.
    IntActiP0ABC7. 11 interactions.
    MINTiMINT-1271770.
    STRINGi511145.b4174.

    Structurei

    3D structure databases

    ProteinModelPortaliP0ABC7.
    SMRiP0ABC7. Positions 128-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 7979Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini101 – 419319Periplasmic1 PublicationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei80 – 10021Helical; Signal-anchor for type II membrane proteinCuratedAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the band 7/mec-2 family. HflK subfamily.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0330.
    HOGENOMiHOG000260983.
    KOiK04088.
    OMAiDPWGKPG.
    OrthoDBiEOG6J48MH.
    PhylomeDBiP0ABC7.

    Family and domain databases

    InterProiIPR001107. Band_7.
    IPR010201. HflK.
    IPR020980. Membrane_HflK_N.
    IPR001972. Stomatin_fam.
    [Graphical view]
    PANTHERiPTHR10264. PTHR10264. 1 hit.
    PTHR10264:SF51. PTHR10264:SF51. 1 hit.
    PfamiPF01145. Band_7. 1 hit.
    PF12221. HflK_N. 1 hit.
    [Graphical view]
    PRINTSiPR00721. STOMATIN.
    SMARTiSM00244. PHB. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01933. hflK. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0ABC7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAWNQPGNNG QDRDPWGSSK PGGNSEGNGN KGGRDQGPPD LDDIFRKLSK    50
    KLGGLGGGKG TGSGGGSSSQ GPRPQLGGRV VTIAAAAIVI IWAASGFYTI 100
    KEAERGVVTR FGKFSHLVEP GLNWKPTFID EVKPVNVEAV RELAASGVML 150
    TSDENVVRVE MNVQYRVTNP EKYLYSVTSP DDSLRQATDS ALRGVIGKYT 200
    MDRILTEGRT VIRSDTQREL EETIRPYDMG ITLLDVNFQA ARPPEEVKAA 250
    FDDAIAAREN EQQYIREAEA YTNEVQPRAN GQAQRILEEA RAYKAQTILE 300
    AQGEVARFAK LLPEYKAAPE ITRERLYIET MEKVLGNTRK VLVNDKGGNL 350
    MVLPLDQMLK GGNAPAAKSD NGASNLLRLP PASSSTTSGA SNTSSTSQGD 400
    IMDQRRANAQ RNDYQRQGE 419
    Length:419
    Mass (Da):45,545
    Last modified:November 8, 2005 - v1
    Checksum:iE7B501DC70A49FBC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00005 Unassigned DNA. Translation: AAC43399.1.
    U14003 Genomic DNA. Translation: AAA97070.1.
    U00096 Genomic DNA. Translation: AAC77131.1.
    AP009048 Genomic DNA. Translation: BAE78175.1.
    PIRiB43653.
    RefSeqiNP_418595.1. NC_000913.3.
    YP_492316.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77131; AAC77131; b4174.
    BAE78175; BAE78175; BAE78175.
    GeneIDi12932259.
    948698.
    KEGGiecj:Y75_p4060.
    eco:b4174.
    PATRICi32123921. VBIEscCol129921_4305.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00005 Unassigned DNA. Translation: AAC43399.1 .
    U14003 Genomic DNA. Translation: AAA97070.1 .
    U00096 Genomic DNA. Translation: AAC77131.1 .
    AP009048 Genomic DNA. Translation: BAE78175.1 .
    PIRi B43653.
    RefSeqi NP_418595.1. NC_000913.3.
    YP_492316.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0ABC7.
    SMRi P0ABC7. Positions 128-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47481N.
    IntActi P0ABC7. 11 interactions.
    MINTi MINT-1271770.
    STRINGi 511145.b4174.

    Protein family/group databases

    MEROPSi I87.002.

    Proteomic databases

    PaxDbi P0ABC7.
    PRIDEi P0ABC7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77131 ; AAC77131 ; b4174 .
    BAE78175 ; BAE78175 ; BAE78175 .
    GeneIDi 12932259.
    948698.
    KEGGi ecj:Y75_p4060.
    eco:b4174.
    PATRICi 32123921. VBIEscCol129921_4305.

    Organism-specific databases

    EchoBASEi EB0431.
    EcoGenei EG10436. hflK.

    Phylogenomic databases

    eggNOGi COG0330.
    HOGENOMi HOG000260983.
    KOi K04088.
    OMAi DPWGKPG.
    OrthoDBi EOG6J48MH.
    PhylomeDBi P0ABC7.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10436-MONOMER.
    ECOL316407:JW4132-MONOMER.
    MetaCyc:EG10436-MONOMER.

    Miscellaneous databases

    PROi P0ABC7.

    Gene expression databases

    Genevestigatori P0ABC7.

    Family and domain databases

    InterProi IPR001107. Band_7.
    IPR010201. HflK.
    IPR020980. Membrane_HflK_N.
    IPR001972. Stomatin_fam.
    [Graphical view ]
    PANTHERi PTHR10264. PTHR10264. 1 hit.
    PTHR10264:SF51. PTHR10264:SF51. 1 hit.
    Pfami PF01145. Band_7. 1 hit.
    PF12221. HflK_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00721. STOMATIN.
    SMARTi SM00244. PHB. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01933. hflK. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain."
      Noble J.A., Innis M.A., Koonin E.V., Rudd K.E., Banuett F., Herskowitz I.
      Proc. Natl. Acad. Sci. U.S.A. 90:10866-10870(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. "Identification of polypeptides encoded by an Escherichia coli locus (hflA) that governs the lysis-lysogeny decision of bacteriophage lambda."
      Banuett F., Herskowitz I.
      J. Bacteriol. 169:4076-4085(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "Cleavage of the cII protein of phage lambda by purified HflA protease: control of the switch between lysis and lysogeny."
      Cheng H.H., Muhlrad P.J., Hoyt M.A., Echols H.
      Proc. Natl. Acad. Sci. U.S.A. 85:7882-7886(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HFLC, SUGGESTION OF PROTEASE ACTIVITY.
      Strain: W3102 and X9368.
    7. "A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY."
      Kihara A., Akiyama Y., Ito K.
      EMBO J. 15:6122-6131(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HFLC AND FTSH, SUBCELLULAR LOCATION, MUTAGENESIS OF ALA-145.
      Strain: K12 / CSH26 / AD16.
    8. "Host regulation of lysogenic decision in bacteriophage lambda: transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA)."
      Kihara A., Akiyama Y., Ito K.
      Proc. Natl. Acad. Sci. U.S.A. 94:5544-5549(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY, LACK OF PROTEASE ACTIVITY.
      Strain: K12 / CSH26 / AD16.
    9. "Translocation, folding, and stability of the HflKC complex with signal anchor topogenic sequences."
      Kihara A., Ito K.
      J. Biol. Chem. 273:29770-29775(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INSTABILITY IN THE ABSENCE OF HFLC, MEMBRANE TRANSLOCATION MECHANISM.
      Strain: K12 / CSH26 / AD16 and K12 / MC4100.
    10. "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: INTERACTION WITH YCCA.
      Strain: K12 / CSH26 / AD16.
    11. "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 nameiHFLK_ECOLI
    AccessioniPrimary (citable) accession number: P0ABC7
    Secondary accession number(s): P25662, Q2M6D1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Integration of this protein into the membrane depends on SecA, SecY and SecD but not on SecB or FtsY. HflK is unstable in the absence of HflC.

    Caution

    Was originally (PubMed:2973057) thought to be a protease. However, removal of residues '165-200' of complex member HflC (a ClpP-protease-like motif) does not alter the lysogenization process, and in vitro studies show no evidence of a protease activity for the isolated HflKC complex.1 Publication

    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

    External Data

    Dasty 3