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protease modulator HflK N-terminal domain-containing protein
This domain is found in bacteria. This domain is typically between 65 to 81 amino acids in length. This domain is found associated with Pfam:PF01145. This domain is the N terminal of the bacterial membrane protein HflK. HflK complexes with HflC to form a membrane protease which is modulated by the GTPase HflX. The N terminal domain of HflK is the membrane spanning region which anchors the protein in the bacterial membrane. [1]. 8248183. The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain. Noble JA, Innis MA, Koonin EV, Rudd KE, Banuett F, Herskowitz I;. Proc Natl Acad Sci U S A. 1993;90:10866-10870. (from Pfam)
SPFH domain-containing protein
This family has been called SPFH [1], Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals. [1]. 10542406. The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins. Tavernarakis N, Driscoll M, Kyrpides NC;. Trends Biochem Sci 1999;24:425-427. [2]. 18267007. Slipins: ancient origin, duplication and diversification of the stomatin protein family. Green JB, Young JP;. BMC Evol Biol. 2008;8:44. (from Pfam)
FtsH protease activity modulator HflK
HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (PMID:8947034,PMID:96367) [SS 8/27/03]
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