HFLK_ECOLI
ID HFLK_ECOLI Reviewed; 419 AA.
AC P0ABC7; P25662; Q2M6D1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Modulator of FtsH protease HflK;
GN Name=hflK; Synonyms=hflA; OrderedLocusNames=b4174, JW4132;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8248183; DOI=10.1073/pnas.90.22.10866;
RA Noble J.A., Innis M.A., Koonin E.V., Rudd K.E., Banuett F., Herskowitz I.;
RT "The Escherichia coli hflA locus encodes a putative GTP-binding protein and
RT two membrane proteins, one of which contains a protease-like domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10866-10870(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION.
RX PubMed=3040675; DOI=10.1128/jb.169.9.4076-4085.1987;
RA Banuett F., Herskowitz I.;
RT "Identification of polypeptides encoded by an Escherichia coli locus (hflA)
RT that governs the lysis-lysogeny decision of bacteriophage lambda.";
RL J. Bacteriol. 169:4076-4085(1987).
RN [6]
RP INTERACTION WITH HFLC, AND SUGGESTION OF PROTEASE ACTIVITY.
RC STRAIN=W3102, and X9368;
RX PubMed=2973057; DOI=10.1073/pnas.85.21.7882;
RA Cheng H.H., Muhlrad P.J., Hoyt M.A., Echols H.;
RT "Cleavage of the cII protein of phage lambda by purified HflA protease:
RT control of the switch between lysis and lysogeny.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7882-7886(1988).
RN [7]
RP FUNCTION, INTERACTION WITH HFLC AND FTSH, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ALA-145.
RC STRAIN=K12 / CSH26 / AD16;
RX PubMed=8947034; DOI=10.1002/j.1460-2075.1996.tb01000.x;
RA Kihara A., Akiyama Y., Ito K.;
RT "A protease complex in the Escherichia coli plasma membrane: HflKC (HflA)
RT forms a complex with FtsH (HflB), regulating its proteolytic activity
RT against SecY.";
RL EMBO J. 15:6122-6131(1996).
RN [8]
RP TOPOLOGY, AND LACK OF PROTEASE ACTIVITY.
RC STRAIN=K12 / CSH26 / AD16;
RX PubMed=9159109; DOI=10.1073/pnas.94.11.5544;
RA Kihara A., Akiyama Y., Ito K.;
RT "Host regulation of lysogenic decision in bacteriophage lambda:
RT transmembrane modulation of FtsH (HflB), the cII degrading protease, by
RT HflKC (HflA).";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5544-5549(1997).
RN [9]
RP INSTABILITY IN THE ABSENCE OF HFLC, AND MEMBRANE TRANSLOCATION MECHANISM.
RC STRAIN=K12 / CSH26 / AD16, and K12 / MC4100;
RX PubMed=9792691; DOI=10.1074/jbc.273.45.29770;
RA Kihara A., Ito K.;
RT "Translocation, folding, and stability of the HflKC complex with signal
RT anchor topogenic sequences.";
RL J. Biol. Chem. 273:29770-29775(1998).
RN [10]
RP INTERACTION WITH YCCA.
RC STRAIN=K12 / CSH26 / AD16;
RX PubMed=9636708; DOI=10.1006/jmbi.1998.1781;
RA Kihara A., Akiyama Y., Ito K.;
RT "Different pathways for protein degradation by the FtsH/HflKC membrane-
RT embedded protease complex: an implication from the interference by a mutant
RT form of a new substrate protein, YccA.";
RL J. Mol. Biol. 279:175-188(1998).
RN [11]
RP REVIEW.
RX PubMed=19454621; DOI=10.1093/jb/mvp071;
RA Akiyama Y.;
RT "Quality control of cytoplasmic membrane proteins in Escherichia coli.";
RL J. Biochem. 146:449-454(2009).
CC -!- FUNCTION: HflC and HflK help govern the stability of phage lambda cII
CC protein, and thereby control the lysogenization frequency of phage
CC lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly
CC helping quality control of integral membrane proteins.
CC {ECO:0000269|PubMed:8947034}.
CC -!- SUBUNIT: HflC and HflK interact to form a complex, originally called
CC HflA, now called HflKC. HflKC interacts with FtsH; complex formation is
CC stimulated by ATP, and with YccA. {ECO:0000269|PubMed:2973057,
CC ECO:0000269|PubMed:8947034, ECO:0000269|PubMed:9636708}.
CC -!- INTERACTION:
CC P0ABC7; P0AAI3: ftsH; NbExp=7; IntAct=EBI-558599, EBI-548381;
CC P0ABC7; P0ABC3: hflC; NbExp=2; IntAct=EBI-558599, EBI-551642;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8947034};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:8947034}.
CC -!- MISCELLANEOUS: Integration of this protein into the membrane depends on
CC SecA, SecY and SecD but not on SecB or FtsY. HflK is unstable in the
CC absence of HflC.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflK subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:2973057) thought to be a protease.
CC However, removal of residues '165-200' of complex member HflC (a ClpP-
CC protease-like motif) does not alter the lysogenization process, and in
CC vitro studies show no evidence of a protease activity for the isolated
CC HflKC complex. {ECO:0000305|PubMed:2973057}.
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DR EMBL; U00005; AAC43399.1; -; Unassigned_DNA.
DR EMBL; U14003; AAA97070.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77131.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78175.1; -; Genomic_DNA.
DR PIR; B43653; B43653.
DR RefSeq; NP_418595.1; NC_000913.3.
DR RefSeq; WP_000312488.1; NZ_STEB01000013.1.
DR AlphaFoldDB; P0ABC7; -.
DR SMR; P0ABC7; -.
DR BioGRID; 4261253; 452.
DR ComplexPortal; CPX-5046; FtsH-HflKC complex.
DR DIP; DIP-47481N; -.
DR IntAct; P0ABC7; 12.
DR MINT; P0ABC7; -.
DR STRING; 511145.b4174; -.
DR MEROPS; I87.002; -.
DR jPOST; P0ABC7; -.
DR PaxDb; P0ABC7; -.
DR PRIDE; P0ABC7; -.
DR EnsemblBacteria; AAC77131; AAC77131; b4174.
DR EnsemblBacteria; BAE78175; BAE78175; BAE78175.
DR GeneID; 60666822; -.
DR GeneID; 67414792; -.
DR GeneID; 948698; -.
DR KEGG; ecj:JW4132; -.
DR KEGG; eco:b4174; -.
DR PATRIC; fig|1411691.4.peg.2527; -.
DR EchoBASE; EB0431; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_039173_1_0_6; -.
DR InParanoid; P0ABC7; -.
DR OMA; WNEPGGN; -.
DR PhylomeDB; P0ABC7; -.
DR BioCyc; EcoCyc:EG10436-MON; -.
DR BioCyc; MetaCyc:EG10436-MON; -.
DR PRO; PR:P0ABC7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098797; C:plasma membrane protein complex; IPI:ComplexPortal.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IDA:ComplexPortal.
DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
DR CDD; cd03404; SPFH_HflK; 1.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR010201; HflK.
DR InterPro; IPR020980; Membrane_HflK_N.
DR InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR PANTHER; PTHR43327:SF2; PTHR43327:SF2; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF12221; HflK_N; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
DR TIGRFAMs; TIGR01933; hflK; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..419
FT /note="Modulator of FtsH protease HflK"
FT /id="PRO_0000094085"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9159109"
FT TRANSMEM 80..100
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 101..419
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9159109"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 145
FT /note="A->V: In hflK13; stabilizes overproduced SecY but
FT not overproduced cII protein."
FT /evidence="ECO:0000269|PubMed:8947034"
SQ SEQUENCE 419 AA; 45545 MW; E7B501DC70A49FBC CRC64;
MAWNQPGNNG QDRDPWGSSK PGGNSEGNGN KGGRDQGPPD LDDIFRKLSK KLGGLGGGKG
TGSGGGSSSQ GPRPQLGGRV VTIAAAAIVI IWAASGFYTI KEAERGVVTR FGKFSHLVEP
GLNWKPTFID EVKPVNVEAV RELAASGVML TSDENVVRVE MNVQYRVTNP EKYLYSVTSP
DDSLRQATDS ALRGVIGKYT MDRILTEGRT VIRSDTQREL EETIRPYDMG ITLLDVNFQA
ARPPEEVKAA FDDAIAAREN EQQYIREAEA YTNEVQPRAN GQAQRILEEA RAYKAQTILE
AQGEVARFAK LLPEYKAAPE ITRERLYIET MEKVLGNTRK VLVNDKGGNL MVLPLDQMLK
GGNAPAAKSD NGASNLLRLP PASSSTTSGA SNTSSTSQGD IMDQRRANAQ RNDYQRQGE
