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P0ABC7 (HFLK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Modulator of FtsH protease HflK
Gene names
Name:hflK
Synonyms:hflA
Ordered Locus Names:b4174, JW4132
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

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. Ref.6 Ref.7 Ref.10

Subcellular location

Cell inner membrane; Single-pass type II membrane protein Ref.7.

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.

Sequence similarities

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

Caution

Was originally (Ref.6) 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Modulator of FtsH protease HflK
PRO_0000094085

Regions

Topological domain1 – 7979Cytoplasmic Ref.8
Transmembrane80 – 10021Helical; Signal-anchor for type II membrane protein; Probable
Topological domain101 – 419319Periplasmic Ref.8

Experimental info

Mutagenesis1451A → V in hflK13; stabilizes overproduced SecY but not overproduced cII protein. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P0ABC7 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: E7B501DC70A49FBC

FASTA41945,545
        10         20         30         40         50         60 
MAWNQPGNNG QDRDPWGSSK PGGNSEGNGN KGGRDQGPPD LDDIFRKLSK KLGGLGGGKG 

        70         80         90        100        110        120 
TGSGGGSSSQ GPRPQLGGRV VTIAAAAIVI IWAASGFYTI KEAERGVVTR FGKFSHLVEP 

       130        140        150        160        170        180 
GLNWKPTFID EVKPVNVEAV RELAASGVML TSDENVVRVE MNVQYRVTNP EKYLYSVTSP 

       190        200        210        220        230        240 
DDSLRQATDS ALRGVIGKYT MDRILTEGRT VIRSDTQREL EETIRPYDMG ITLLDVNFQA 

       250        260        270        280        290        300 
ARPPEEVKAA FDDAIAAREN EQQYIREAEA YTNEVQPRAN GQAQRILEEA RAYKAQTILE 

       310        320        330        340        350        360 
AQGEVARFAK LLPEYKAAPE ITRERLYIET MEKVLGNTRK VLVNDKGGNL MVLPLDQMLK 

       370        380        390        400        410 
GGNAPAAKSD NGASNLLRLP PASSSTTSGA SNTSSTSQGD IMDQRRANAQ RNDYQRQGE 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00005 Unassigned DNA. Translation: AAC43399.1.
U14003 Genomic DNA. Translation: AAA97070.1.
U00096 Genomic DNA. Translation: AAC77131.1.
AP009048 Genomic DNA. Translation: BAE78175.1.
PIRB43653.
RefSeqNP_418595.1. NC_000913.3.
YP_492316.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0ABC7.
SMRP0ABC7. Positions 128-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47481N.
IntActP0ABC7. 11 interactions.
MINTMINT-1271770.
STRING511145.b4174.

Protein family/group databases

MEROPSI87.002.

Proteomic databases

PaxDbP0ABC7.
PRIDEP0ABC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77131; AAC77131; b4174.
BAE78175; BAE78175; BAE78175.
GeneID12932259.
948698.
KEGGecj:Y75_p4060.
eco:b4174.
PATRIC32123921. VBIEscCol129921_4305.

Organism-specific databases

EchoBASEEB0431.
EcoGeneEG10436. hflK.

Phylogenomic databases

eggNOGCOG0330.
HOGENOMHOG000260983.
KOK04088.
OMAWNEPGGN.
OrthoDBEOG6J48MH.
PhylomeDBP0ABC7.
ProtClustDBPRK10930.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0ABC7.

Family and domain databases

InterProIPR001107. Band_7.
IPR010201. HflK.
IPR020980. Membrane_HflK_N.
IPR001972. Stomatin_fam.
[Graphical view]
PANTHERPTHR10264. PTHR10264. 1 hit.
PTHR10264:SF51. PTHR10264:SF51. 1 hit.
PfamPF01145. Band_7. 1 hit.
PF12221. HflK_N. 1 hit.
[Graphical view]
PRINTSPR00721. STOMATIN.
SMARTSM00244. PHB. 1 hit.
[Graphical view]
TIGRFAMsTIGR01933. hflK. 1 hit.
ProtoNetSearch...

Other

PROP0ABC7.

Entry information

Entry nameHFLK_ECOLI
AccessionPrimary (citable) accession number: P0ABC7
Secondary accession number(s): P25662, Q2M6D1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

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