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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

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • metabolic process Source: GOC
  • regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, 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
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU15280. [Micado]

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

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

eggNOGiCOG0849.
HOGENOMiHOG000049205.
InParanoidiP28264.
KOiK03590.
OMAiHTAVIPF.
OrthoDBiEOG6TR0B6.
PhylomeDBiP28264.

Family and domain databases

HAMAPiMF_02033. FtsA.
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.

Organism-specific databases

GenoListiBSU15280. [Micado]

Phylogenomic databases

eggNOGiCOG0849.
HOGENOMiHOG000049205.
InParanoidiP28264.
KOiK03590.
OMAiHTAVIPF.
OrthoDBiEOG6TR0B6.
PhylomeDBiP28264.

Enzyme and pathway databases

BioCyciBSUB:BSU15280-MONOMER.

Family and domain databases

HAMAPiMF_02033. FtsA.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of Bacillus subtilis homologs of Escherichia coli cell division genes ftsZ and ftsA."
    Beall B., Lowe M., Lutkenhaus J.
    J. Bacteriol. 170:4855-4864(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 12; 26; 112 AND 349-350.
  4. "Developmental regulation of transcription of the Bacillus subtilis ftsAZ operon."
    Gonzy-Treboul G., Karmazyn-Campelli C., Stragier P.
    J. Mol. Biol. 224:967-979(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14, INDUCTION.
    Strain: 168 / JH642.
  5. "Regulation of transcription of the cell division gene ftsA during sporulation of Bacillus subtilis."
    Gholamhoseinian A., Shen Z., Wu J.J., Piggot P.
    J. Bacteriol. 174:4647-4656(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, INDUCTION.
  6. "Cytological and biochemical characterization of the FtsA cell division protein of Bacillus subtilis."
    Feucht A., Lucet I., Yudkin M.D., Errington J.
    Mol. Microbiol. 40:115-125(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  7. "Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly."
    Jensen S.O., Thompson L.S., Harry E.J.
    J. Bacteriol. 187:6536-6544(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FTSZ.

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: July 22, 2015
This is version 101 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

External Data

Dasty 3

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 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.