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| * '''Description:''' preprotein translocase subunit (ATPase), required for membrane targeting of [[DivIVA]], motor protein that drives preprotein translocation through the [[SecY]]-[[SecE]]-[[SecG]] channel <br/><br/>
| | {{#bank: SecA}} |
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| {| align="right" border="1" cellpadding="2"
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| |style="background:#ABCDEF;" align="center"|'''Gene name'''
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| |''secA''
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| |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''div, div-341, ts-341 ''
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| |style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
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| |style="background:#ABCDEF;" align="center"| '''Product''' || preprotein translocase subunit (ATPase)
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| |style="background:#ABCDEF;" align="center"|'''Function''' || [[protein secretion]]
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| |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU35300 secA]
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| |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=SecA SecA]
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| |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=SecA SecA]'''
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| |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 95 kDa, 5.34
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| |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 2523 bp, 841 aa
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| |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[prfB]]'', ''[[yvyD]]''
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| |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU35300 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU35300 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU35300 DNA_with_flanks]
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| |colspan="2" | '''Genetic context''' <br/> [[Image:secA_context.gif]]
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| <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
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| |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=secA_3628310_3630835_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:secA_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU35300]]
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| |-
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| |}
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| __TOC__
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| <br/><br/><br/><br/>
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| <br/><br/><br/><br/>
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| <br/><br/><br/><br/>
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| <br/><br/>
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| = [[Categories]] containing this gene/protein =
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| {{SubtiWiki category|[[protein secretion]]}},
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| {{SubtiWiki category|[[essential genes]]}},
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| {{SubtiWiki category|[[membrane proteins]]}}
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| = This gene is a member of the following [[regulons]] =
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| =The gene=
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| === Basic information ===
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| * '''Locus tag:''' BSU35300
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| ===Phenotypes of a mutant ===
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| essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
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| === Database entries ===
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| * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU35300&redirect=T BSU35300]
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| * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/secA-prfB.html]
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| * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10741]
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| === Additional information===
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| =The protein=
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| === Basic information/ Evolution ===
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| * '''Catalyzed reaction/ biological activity:'''
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| ** ATP -> ADP + Pi + preprotein translocation
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| ** required for membrane targeting of [[DivIVA]] {{PubMed|24592260}}
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| * '''Protein family:''' SecA family (according to Swiss-Prot)
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| * '''Paralogous protein(s):''' none in Bacillus, some species have a paralogous secA gene named secA2 that has an altered substrate range
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| === Extended information on the protein ===
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| * '''Kinetic information:'''
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| * '''[[Domains]]:''' nucleotide binding domain, preprotein binding domain, IRA2 domain, scaffold domain, wing domain, IRA1 domain, C-terminal domain
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| * '''Modification:'''
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| * '''[[Cofactors]]:''' Mg
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| * '''Effectors of protein activity:''' anionic phospholipids, preprotein, [[SecY]], signal peptides (even when added in trans) [http://www.ncbi.nlm.nih.gov/pubmed/19924216 PubMed]
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| * '''[[SubtInteract|Interactions]]:'''
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| ** ([[SecY]]-[[SecE]]-[[SecG]])2-[[SecA]]2 {{PubMed|18923516}}
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| ** [[SecA]]-[[Ffh]] {{PubMed|9880811}}
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| ** [[CsaA]]-[[SecA]] {{PubMed|10816431}}
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| ** [[DivIVA]]-[[SecA]] {{PubMed|24592260}}
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| * '''[[Localization]]:''' cell membrane (according to Swiss-Prot)
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| === Database entries ===
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| * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU35300&redirect=T BSU35300]
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| * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1TF5 1TF5] (open structure), [http://www.rcsb.org/pdb/explore.do?structureId=2IBM 2IBM], [http://www.rcsb.org/pdb/explore/explore.do?pdbId=3DL8 3DL8] (structure of the ([[SecY]]-[[SecE]]-[[SecG]])-[[SecA]] complex {{PubMed|18923516}}
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| * '''UniProt:''' [http://www.uniprot.org/uniprot/P28366 P28366]
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| * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU35300]
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| * '''E.C. number:'''
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| === Additional information===
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| * subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
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| =Expression and regulation=
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| * '''Operon:''' ''[[secA]]-[[prfB]]'' {{PubMed|9882663}}
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| * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=secA_3628310_3630835_-1 secA] {{PubMed|22383849}}
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| * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|9882663}}
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| * '''Regulation:'''
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| * '''Regulatory mechanism:'''
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| * '''Additional information:'''
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| ** subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
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| ** number of protein molecules per cell (minimal medium with glucose and ammonium): 945 {{PubMed|24696501}}
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| ** number of protein molecules per cell (complex medium with amino acids, without glucose): 2829 {{PubMed|24696501}}
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| ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 411 {{PubMed|21395229}}
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| ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 395 {{PubMed|21395229}}
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| ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 564 {{PubMed|21395229}}
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| =Biological materials =
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| * '''Mutant: ''Pspac-[[secA]]'' [http://www.ncbi.nlm.nih.gov/pubmed/12218047 PubMed]
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| * '''Expression vector:'''
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| * '''lacZ fusion:'''
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| * '''GFP fusion:'''
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| * '''two-hybrid system:'''
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| * '''Antibody:'''
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| =Labs working on this gene/protein=
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| =Your additional remarks=
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| =References=
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| <pubmed>19933328, 19924216, 18923516,12873133, 12242434,1385592,10816431,19850053,9880811, 12218047 17981983 9882663 23484952 20574771 23167435 23794293 23852076 24592260 24786965 11021932 7851746 7894702 10074074 8497195 8440733 7706219 7642557 </pubmed>
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| [[Category:Protein-coding genes]]
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