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HAMAP rule MF_01458

General rule information [?]

Accession	MF_01458
Dates	13-SEP-2010 (Created) 1-JUN-2023 (Last updated, Version 14)
Name	FtsH
Scope(s)	Bacteria Plastid
Template(s)	P0AAI3 (FTSH_ECOLI); O67077 (FTSH_AQUAE); Q9WZ49 (FTSH_THEMA); Q5SI82 (FTSH_THET8); Q55700 (FTSH2_SYNY3); [ Recover all ]
Triggered by	HAMAP; MF_01458 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier	FTSH
Protein name	RecName: Full=ATP-dependent zinc metalloprotease FtsH; EC=3.4.24.-;
Gene name	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	Name=Zn(2+); Xref=ChEBI:CHEBI:29105; 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.
SIMILARITY	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 <OCellular component:Cyanobacteriota> and not <OC:Gloeobacter>
GO:0042651; Cellular component:thylakoid membrane
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0005886; Cellular component:plasma membrane
end case

Cross-references [?]

Features [?]

From: FTSH_AQUAE (O67077)

Key

From

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

BINDING

418

/ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="catalytic"

BINDING

422

/ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="catalytic"

BINDING

496

/ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="catalytic"

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).