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Protein

Cell division protein FtsA

Gene

ftsA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Cell division protein that is required for the assembly of the Z ring (PubMed:16159787). May serve as a membrane anchor for the Z ring (By similarity). Binds and hydrolyzes ATP (PubMed:11298280). Also involved in sporulation (Probable).By similarity2 Publications2 Publications

GO - Molecular functioni

  • ATPase activity Source: CACAO

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU15280-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsAUniRule annotation
Gene namesi
Name:ftsAUniRule annotation
Ordered Locus Names:BSU15280
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

  • Note: Localizes to the Z ring in an FtsZ-dependent manner (PubMed:11298280). In sporulating cells, preferentially localizes to only one of the two potential polar division sites (PubMed:11298280). Targeted to the membrane through a conserved C-terminal amphiphatic helix (By similarity).By similarity1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Cell division protein FtsAPRO_0000062729Add
BLAST

Proteomic databases

PaxDbiP28264.

Expressioni

Inductioni

Transcription is controlled by three promoters. Two of these promoters, P1 and P3 are expressed mainly during vegetative growth. The third one, P2, is up-regulated around the onset of sporulation.2 Publications

Interactioni

Subunit structurei

Homodimer (PubMed:11298280). Interacts with FtsZ (PubMed:16159787).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ezrAO348945EBI-2122615,EBI-1567579
ftsZP178657EBI-2122615,EBI-1569853

Protein-protein interaction databases

IntActiP28264. 25 interactions.
MINTiMINT-1527318.
STRINGi224308.Bsubs1_010100008456.

Structurei

3D structure databases

ProteinModelPortaliP28264.
SMRiP28264. Positions 3-371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsA/MreB family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105CIT. Bacteria.
COG0849. LUCA.
HOGENOMiHOG000049205.
InParanoidiP28264.
KOiK03590.
OMAiVIPFGGN.
PhylomeDBiP28264.

Family and domain databases

HAMAPiMF_02033. FtsA. 1 hit.
InterProiIPR020823. Cell_div_FtsA.
IPR003494. SHS2_FtsA.
[Graphical view]
PfamiPF02491. SHS2_FTSA. 1 hit.
[Graphical view]
PIRSFiPIRSF003101. FtsA. 1 hit.
SMARTiSM00842. FtsA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01174. ftsA. 1 hit.

Sequencei

Sequence statusi: Complete.

P28264-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNNELYVSL DIGTSNTKVI VGEMTDDSLN IIGVGNVPSE GLKKGSIVDI
60 70 80 90 100
DETVHSIRKA FDQAERMVGF PLRKAIVGVN GNYINIQDTN GVVAVSSENK
110 120 130 140 150
EIQVEDVRRV MEAAQVVSVP HEQLIVDVIP KQFIVDGRDE ITDPKKMLGV
160 170 180 190 200
RLEVEGTLIT GSKTILHNLL RCVERAGIEI TDICLQPLAA GSAALSKDEK
210 220 230 240 250
NLGVALIDIG GGSTTIAVFQ NGHLTSTRVI PLGGENITKD ISIGLRTSTE
260 270 280 290 300
EAERVKKQLG HAYYDEASED EIFEVTVIGT NQKQTFTQQE AANIIEARVE
310 320 330 340 350
EILEIVSEEL RSMGITDLPG GFVLTGGQAA MPGVMSLAQD VLQNNVRVAS
360 370 380 390 400
PNYIGVRDPQ YMTGVGLIQF ACRNARIQGR KIGFKMPEEA IQEIAVSSSE
410 420 430 440
EQEQHHHQNE VQQRPKGKQK TQAEHNKQSK MKKLLSMFWE
Length:440
Mass (Da):48,192
Last modified:June 16, 2009 - v2
Checksum:i4BF656A8C71BF15A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121I → L in AAA22456 (PubMed:3139638).Curated
Sequence conflicti26 – 261D → G in AAA22456 (PubMed:3139638).Curated
Sequence conflicti112 – 1121E → A in AAA22456 (PubMed:3139638).Curated
Sequence conflicti349 – 3502AS → QG in AAA22456 (PubMed:3139638).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22630 Genomic DNA. Translation: AAA22456.1.
AL009126 Genomic DNA. Translation: CAB13401.2.
X66239 Genomic DNA. Translation: CAA46968.1.
S39431 Genomic DNA. Translation: AAD13818.1.
PIRiI39847.
RefSeqiNP_389411.2. NC_000964.3.
WP_009967186.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13401; CAB13401; BSU15280.
GeneIDi936145.
KEGGibsu:BSU15280.
PATRICi18974861. VBIBacSub10457_1622.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22630 Genomic DNA. Translation: AAA22456.1.
AL009126 Genomic DNA. Translation: CAB13401.2.
X66239 Genomic DNA. Translation: CAA46968.1.
S39431 Genomic DNA. Translation: AAD13818.1.
PIRiI39847.
RefSeqiNP_389411.2. NC_000964.3.
WP_009967186.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP28264.
SMRiP28264. Positions 3-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28264. 25 interactions.
MINTiMINT-1527318.
STRINGi224308.Bsubs1_010100008456.

Proteomic databases

PaxDbiP28264.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13401; CAB13401; BSU15280.
GeneIDi936145.
KEGGibsu:BSU15280.
PATRICi18974861. VBIBacSub10457_1622.

Phylogenomic databases

eggNOGiENOG4105CIT. Bacteria.
COG0849. LUCA.
HOGENOMiHOG000049205.
InParanoidiP28264.
KOiK03590.
OMAiVIPFGGN.
PhylomeDBiP28264.

Enzyme and pathway databases

BioCyciBSUB:BSU15280-MONOMER.

Family and domain databases

HAMAPiMF_02033. FtsA. 1 hit.
InterProiIPR020823. Cell_div_FtsA.
IPR003494. SHS2_FtsA.
[Graphical view]
PfamiPF02491. SHS2_FTSA. 1 hit.
[Graphical view]
PIRSFiPIRSF003101. FtsA. 1 hit.
SMARTiSM00842. FtsA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01174. ftsA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFTSA_BACSU
AccessioniPrimary (citable) accession number: P28264
Secondary accession number(s): Q45573
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 16, 2009
Last modified: September 7, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In B.subtilis, unlike the situation in E.coli, the role of FtsA in the recruitment of other division proteins to the division site appears to be an indirect one, through ensuring that FtsZ forms a proper ring.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.