HAMAP rule MF_01458
General rule information
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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
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
Gene name |
|
Comments
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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
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case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter>
else case (defined <Property:Membrane> and <Property:Membrane=2>) or <OC:Gloeobacter>
else case not defined <Property:Membrane> or <Property:Membrane=1>
end case
Hydrolase
Membrane
Metal-binding
Metalloprotease
Nucleotide-binding
Protease
Transmembrane
Transmembrane helix
Zinc
Membrane
Metal-binding
Metalloprotease
Nucleotide-binding
Protease
Transmembrane
Transmembrane helix
Zinc
Gene Ontology
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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.
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
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PROSITE | PS00674; AAA; 1; |
Pfam | PF00004; AAA; 1; |
PF06480; FtsH_ext; 1; | |
PF01434; Peptidase_M41; 1; | |
NCBIfam | TIGR01241; FtsH_fam; 1; |
Computed features
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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
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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
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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). |