HAMAP rule MF_01382
General rule information
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Accession | MF_01382 |
Dates | 14-JAN-2008 (Created)
1-JUN-2023 (Last updated, Version 36) |
Name | SecA |
Scope(s) |
Bacteria Plastid |
Template(s) | P10408 (SECA_ECOLI); P28366 (SECA_BACSU); P43803 (SECA_HAEIN); [ Recover all ] |
Triggered by |
HAMAP; MF_01382 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | SECA |
RecName: Full=Protein translocase subunit SecA;<br /> EC=<a href="https://enzyme.expasy.org/EC/7.4.2.8">7.4.2.8</a>; | |
Gene name | Name=secA; |
Comments
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case <OG:Chloroplast> | |
FUNCTION | Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane. |
else case <OC:Alphaproteobacteria> or <OC:Betaproteobacteria> or <OC:Gammaproteobacteria> | |
FUNCTION | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. |
else | |
FUNCTION | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. |
end case | |
case <OC:Cyanobacteriota> and not <OC:Gloeobacter> | |
FUNCTION | Probably participates in protein translocation into and across both the cytoplasmic and thylakoid membranes in cyanobacterial cells. |
end case | |
CATALYTIC ACTIVITY | Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.; EC=7.4.2.8; |
case <FTGroup:1> | |
COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=May bind 1 zinc ion per subunit.; |
end case | |
case <OC:Pseudomonadota> | |
SUBUNIT | Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC. |
else case not <OG:Chloroplast> | |
SUBUNIT | Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved. |
end case | |
case <OG:Chloroplast> | |
SUBCELLULAR LOCATION | Plastid, chloroplast stroma. Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. Note=A minor fraction is associated with the chloroplast thylakoid membrane. |
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter> | |
SUBCELLULAR LOCATION | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. |
else case <OC:Gloeobacter> | |
SUBCELLULAR LOCATION | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Note=Distribution is 50-50. |
else case not defined <Property:Membrane> or <Property:Membrane=1> | |
SUBCELLULAR LOCATION | Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Note=Distribution is 50-50. |
else case <Property:Membrane=2> | |
SUBCELLULAR LOCATION | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Note=Distribution is 50-50. |
end case | |
case <OC:Enterobacterales> | |
INDUCTION | Repressed under conditions of excess protein secretion capacity and derepressed when protein secretion becomes limiting. This is regulated by SecM. |
end case | |
SIMILARITY | Belongs to the SecA family. |
Keywords
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ATP-binding | |
case not <OG:Chloroplast> | |
Cytoplasm | |
end case | |
case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter> | |
Thylakoid | |
else case <OC:Gloeobacter> | |
Cell membrane | |
Cell inner membrane | |
else case not defined <Property:Membrane> or <Property:Membrane=1> | |
Cell membrane | |
else case <Property:Membrane=2> | |
Cell membrane | |
Cell inner membrane | |
end case | |
Membrane | |
case <FTGroup:1> | |
Metal-binding | |
Zinc | |
end case | |
Nucleotide-binding | |
Protein transport | |
<a href="https://www.uniprot.org/keywords/KW-1278">Translocase</a> | |
Translocation | |
Transport |
Gene Ontology
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GO:0005524; Molecular function:ATP binding | |
GO:0065002; Biological process:intracellular protein transmembrane transport | |
GO:0006605; Biological process:protein targeting | |
case <OG:Chloroplast> | |
GO:0009570; Cellular component:chloroplast stroma | |
GO:0009535; Cellular component:chloroplast thylakoid membrane | |
else; https://www.ebi.ac.uk/QuickGO/term/else | |
GO:0005886; Cellular component:plasma membrane | |
end case | |
case <OCellular component:Cyanobacteriota> and not <OC:Gloeobacter> | |
GO:0042651; Cellular component:thylakoid membrane | |
end case |
Cross-references
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PROSITE | PS01312; SECA; 1; |
PROSITE | PS51196; SECA_MOTOR_DEAD; 1; |
Pfam | PF07517; SecA_DEAD; 1; |
Pfam | PF01043; SecA_PP_bind; 1; |
Pfam | PF07516; SecA_SW; 1; |
Pfam | PF02810; SEC-C; 1; |
PRINTS | PR00906; SECA; 1; |
NCBIfam | TIGR00963; SecA; 1; |
Features
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From: SECA_BACSU (P28366) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 103 | 107 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G-E-G-K-[TS] | ||||||||
BINDING | 825 | 825 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
BINDING | 827 | 827 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
BINDING | 836 | 836 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
BINDING | 837 | 837 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
[CH] | 1 | |||||||
BINDING | 85 | 85 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
Q | ||||||||
BINDING | 492 | 492 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
D |
Additional information
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Size range | 649-1160 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: <Unknown> |
Comments | It is not yet clear whether the form that inserts preproteins into the membrane in conjunction with SecYEG is monmeric or dimeric. In some bacteria that have 2 copies (Listeria, Mycobacteria), 1 copy (secA1) is thought to be essential whereas the other (secA2) is required only for translocation of a subset of proteins. Mycobacteria have 2 copies, with the exception of MYCA1 which only has a copy of secA2. MALP2 has a C- terminal extension that resembles nothing in the database. SECA1_RHOBA (AC Q7UDY6) has a few short inserts compared to other sequences; its length has not been taken into account in the size range. In BAUCH (BCI_0515) it is annotated as a pseudogene with a verfied point mutation leading to a slightly truncated protein. Not encoded in CARRP. |