HFLC_ECOLI » Modulator of FtsH protease HflC

HFLC_ECOLI » Modulator of FtsH protease HflC
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Topology in Bacterial Gram-negative inner membrane
Topologyextracellular side
cytoplasmic side
HFLC_ECOLI » Modulator of FtsH protease HflC »
Hydrophobic Thickness 32.4 ± 2.8 Å
Tilt Angle 0 ± 1°
ΔGtransfer -36.1 kcal/mol
ΔGfold -17.6 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING
Topology In
TM Segments 3-26 (2-28)
Pathways none
PDB none
OPM none
Complexes none
Interactions

FTSH, Complex: HFLC:FTSH, PubMed

Domains

AA: 21-251, PDBID: 4FVF, Subunit A, Seq Identity:24%, SPFH domain / Band 7 family

UniProt annotation for HFLC_ECOLI » Modulator of FtsH protease HflC
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.

SUBUNIT: 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.

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

UniProt features for HFLC_ECOLI » Modulator of FtsH protease HflC
CHAIN 1 334 Modulator of FtsH protease HflC.
Amino Acid Sequence for HFLC_ECOLI » Modulator of FtsH protease HflC
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