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P0ABC7

- HFLK_ECOLI

UniProt

P0ABC7 - HFLK_ECOLI

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Protein

Modulator of FtsH protease HflK

Gene
hflK, hflA, b4174, JW4132
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7979Cytoplasmic1 PublicationAdd
BLAST
Transmembranei80 – 10021Helical; Signal-anchor for type II membrane protein; InferredAdd
BLAST
Topological domaini101 – 419319Periplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

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

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.

Family & Domainsi

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 72 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 (1 Publication) 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.

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

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