HFLC_ECOLI
ID HFLC_ECOLI Reviewed; 334 AA.
AC P0ABC3; P25661; Q2M6D0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Modulator of FtsH protease HflC;
GN Name=hflC; Synonyms=hflA; OrderedLocusNames=b4175, JW4133;
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 HFLK, 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 HFLK AND FTSH, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-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, LACK OF PROTEASE ACTIVITY, AND MUTAGENESIS OF 165-GLU--ALA-200.
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 HFLK, 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 P0ABC3; P0AAI3: ftsH; NbExp=9; IntAct=EBI-551642, EBI-548381;
CC P0ABC3; P0ABC7: hflK; NbExp=2; IntAct=EBI-551642, EBI-558599;
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. HflC is unstable in the
CC absence of HflK.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:2973057) thought to be a protease.
CC However, removal of residues 165-200 (a ClpP-protease-like motif) does
CC not alter the lysogenization process, and in vitro studies show no
CC evidence of a protease activity for the isolated HflKC complex.
CC {ECO:0000305|PubMed:2973057}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00005; AAC43400.1; -; Unassigned_DNA.
DR EMBL; U14003; AAA97071.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77132.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78176.1; -; Genomic_DNA.
DR PIR; C43653; C43653.
DR RefSeq; NP_418596.1; NC_000913.3.
DR RefSeq; WP_001232412.1; NZ_STEB01000013.1.
DR AlphaFoldDB; P0ABC3; -.
DR SMR; P0ABC3; -.
DR BioGRID; 4262706; 214.
DR ComplexPortal; CPX-5046; FtsH-HflKC complex.
DR DIP; DIP-35995N; -.
DR IntAct; P0ABC3; 9.
DR MINT; P0ABC3; -.
DR STRING; 511145.b4175; -.
DR MEROPS; I87.001; -.
DR jPOST; P0ABC3; -.
DR PaxDb; P0ABC3; -.
DR PRIDE; P0ABC3; -.
DR EnsemblBacteria; AAC77132; AAC77132; b4175.
DR EnsemblBacteria; BAE78176; BAE78176; BAE78176.
DR GeneID; 66671912; -.
DR GeneID; 948697; -.
DR KEGG; ecj:JW4133; -.
DR KEGG; eco:b4175; -.
DR PATRIC; fig|1411691.4.peg.2526; -.
DR EchoBASE; EB0430; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_059167_3_0_6; -.
DR InParanoid; P0ABC3; -.
DR OMA; DFFAFYR; -.
DR PhylomeDB; P0ABC3; -.
DR BioCyc; EcoCyc:EG10435-MON; -.
DR BioCyc; MetaCyc:EG10435-MON; -.
DR PRO; PR:P0ABC3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; IDA:EcoCyc.
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:EcoCyc.
DR CDD; cd03405; SPFH_HflC; 1.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR010200; HflC.
DR PANTHER; PTHR42911; PTHR42911; 1.
DR Pfam; PF01145; Band_7; 1.
DR PIRSF; PIRSF005651; HflC; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 2.
DR TIGRFAMs; TIGR01932; hflC; 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..334
FT /note="Modulator of FtsH protease HflC"
FT /id="PRO_0000094073"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9159109"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 24..334
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9159109"
FT MUTAGEN 145
FT /note="G->A: In hflC9; stabilizes overproduced SecY but not
FT overproduced cII protein."
FT /evidence="ECO:0000269|PubMed:8947034"
FT MUTAGEN 165..200
FT /note="Missing: No effect on phage lambda lysogenization
FT frequency."
FT /evidence="ECO:0000269|PubMed:9159109"
SQ SEQUENCE 334 AA; 37650 MW; FC2B0AAC65D27946 CRC64;
MRKSVIAIII IVLVVLYMSV FVVKEGERGI TLRFGKVLRD DDNKPLVYEP GLHFKIPFIE
TVKMLDARIQ TMDNQADRFV TKEKKDLIVD SYIKWRISDF SRYYLATGGG DISQAEVLLK
RKFSDRLRSE IGRLDVKDIV TDSRGRLTLE VRDALNSGSA GTEDEVTTPA ADNAIAEAAE
RVTAETKGKV PVINPNSMAA LGIEVVDVRI KQINLPTEVS EAIYNRMRAE REAVARRHRS
QGQEEAEKLR ATADYEVTRT LAEAERQGRI MRGEGDAEAA KLFADAFSKD PDFYAFIRSL
RAYENSFSGN QDVMVMSPDS DFFRYMKTPT SATR
