Annotation rule MF_01458
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General rule information [?]

Accession MF_01458
Dates 13-SEP-2010 (Created)
29-SEP-2010 (Last updated, Version 2)
Name FtsH
Scope Bacteria
Plastid
Templates P0AAI3 (FTSH_ECOLI); O67077 (FTSH_AQUAE); Q9WZ49 (FTSH_THEMA); Q5SI82 (FTSH_THET8); Q55700 (FTSH2_SYNY3): [Recover all]

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 (By similarity).
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 (By similarity).
end case
case <FTGroup:1>
Cofactor Binds 1 zinc ion per subunit (By similarity).
end case
Subunit Homohexamer (Potential).
case <OG:Chloroplast>
Subcellular location Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein; Stromal side (Potential).
else case <OC:Cyanobacteria> and not <OC:Gloeobacter>
Subcellular location Cellular thylakoid membrane; Multi-pass membrane protein; Stromal side (By similarity).
else case <OC:Gloeobacter>
Subcellular location Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side (Potential).
else case not defined <Property:Membrane> or <Property:Membrane=1>
Subcellular location Cell membrane; Multi-pass membrane protein; Cytoplasmic side (By similarity).
else case <Property:Membrane=2>
Subcellular location Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side (By similarity).
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 [?]

case <OG:Chloroplast> or <OC:Cyanobacteria> and not <OC:Gloeobacter>
else case <OC:Gloeobacter>
else case not defined <Property:Membrane> or <Property:Membrane=1>
else case <Property:Membrane=2>
end case

Gene Ontology [?]

GO:0005524; Molecular function: ATP binding.
GO:0016887; Molecular function: ATPase 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.

Keywords [?]

else case <OC:Cyanobacteria> and not <OC:Gloeobacter>
else case <OC:Gloeobacter>
else case not defined <Property:Membrane> or <Property:Membrane=1>
else case <Property:Membrane=2>
end case

Cross-references [?]

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

Computed features [?]

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

Features [?]

From: FTSH_AQUAE (O67077)
Key     From     To       Description   Tag   Condition   FTGroup
NP_BIND     195     202       ATP (Potential)     G-x-[PT]-G-[TVS]-G-K-T  
ACT_SITE     419     419       By similarity     E  
METAL     418     418       Zinc; catalytic (By similarity)     H   1
METAL     422     422       Zinc; catalytic (By similarity)     H   1
METAL     496     496       Zinc; catalytic (By similarity)     D   1

Additional information [?]

Size range 510-854 amino acids
Related rules None
Fusion Nter: <Unknown>; Cter: None
Comments Chlamydiae 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 (CHLVUHELSJ, OLTVI).