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HAMAP rule MF_01458

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General rule information [?]

Accession MF_01458
Dates 13-SEP-2010 (Created)
1-JUN-2023 (Last updated, Version 14)
Name FtsH
Scope
Bacteria
Plastid
Templates P0AAI3 (FTSH_ECOLI); O67077 (FTSH_AQUAE); Q9WZ49 (FTSH_THEMA); Q5SI82 (FTSH_THET8); Q55700 (FTSH2_SYNY3): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
FTSH
Protein name
RecName: Full=ATP-dependent zinc metalloprotease FtsH;
EC 3.4.24.-;
Gene name
ftsH

Comments [?]

case <OG:Chloroplast>
Function Acts as a processive, ATP-dependent zinc metallopeptidase.
else
Function Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
end case
case <FTGroup:1>
Cofactor Zn(2+)
Note: Binds 1 zinc ion per subunit.
end case
Subunit Homohexamer.
case <OG:Chloroplast>
Subcellular location Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein; Stromal side.
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
Subcellular location Cellular thylakoid membrane; Multi-pass membrane protein; Stromal side.
else case (defined <Property:Membrane> and <Property:Membrane=2>) or <OC:Gloeobacter>
Subcellular location Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side.
else case not defined <Property:Membrane> or <Property:Membrane=1>
Subcellular location Cell membrane; Multi-pass membrane protein; Cytoplasmic side.
end case
Similarity In the central section; belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.

Keywords [?]

ATP-binding
case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter>
Thylakoid
else case (defined <Property:Membrane> and <Property:Membrane=2>) or <OC:Gloeobacter>
Cell inner membrane
Cell membrane
else case not defined <Property:Membrane> or <Property:Membrane=1>
Cell membrane
end case
Hydrolase
Membrane
Metal-binding
Metalloprotease
Nucleotide-binding
Protease
Transmembrane
Transmembrane helix
Zinc

Gene Ontology [?]

GO:0005524; Molecular function: ATP binding.
GO:0016887; Molecular function: ATP hydrolysis activity.
GO:0008233; Molecular function: peptidase activity.
GO:0030163; Biological process: protein catabolic process.
case <FTGroup:1>
GO:0008270; Molecular function: zinc ion binding.
end case
case <OG:Chloroplast>
GO:0009535; Cellular component: chloroplast thylakoid membrane.
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
GO:0042651; Cellular component: thylakoid membrane.
else
GO:0005886; Cellular component: plasma membrane.
end case

Cross-references [?]

PROSITE PS00674; AAA; 1;
Pfam PF00004; AAA; 1;
PF06480; FtsH_ext; 1;
PF01434; Peptidase_M41; 1;
NCBIfam TIGR01241; FtsH_fam; 1;

Computed features [?]

General Transmembrane; -; 2; trigger=yes;
case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
ADD_TOPO_DOMAIN Cytoplasmic; -; 2; trigger=yes;
Lumenal; -; 1; trigger=yes;
else case <OG:Chloroplast>
Stromal; -; 2; trigger=yes;
Lumenal; -; 1; trigger=yes;
else case (defined <Property:Membrane> and <Property:Membrane=2>) or <OC:Gloeobacter>
Cytoplasmic; -; 2; trigger=yes;
Periplasmic; -; 1; trigger=yes;
else case not defined <Property:Membrane> or <Property:Membrane=1>
Cytoplasmic; -; 2; trigger=yes;
Extracellular; -; 1; trigger=yes;
end case

Features [?]

From: FTSH_AQUAE (O67077)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     195     202       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     G-x-[PT]-G-[TVS]-G-K-T  
ACT_SITE     419     419             E  
BINDING     418     418       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic     H   1
BINDING     422     422       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic     H   1
BINDING     496     496       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic     D   1

Additional information [?]

Size range 510-854 amino acids
Related rules None
Fusion Nter: <Unknown>; Cter: None
Comments Chlamydiota have an N-terminal extension not found in other organisms. Not all proteins have 2 transmembrane domains. There are short paralogs in Haemophilus that are missing the N-terminal transmembrane section, they are annotated as atypical. Some plastids encode very long homologs that cannot bind zinc, they are annotated as atypical (CHLVU, HELSJ, OLTVI).


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