Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cell division protein FtsA

Gene

ftsA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential cell division protein that assists in the assembly of the Z ring (PubMed:11847116). May serve as the principal membrane anchor for the Z ring (PubMed:15752196). Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN (PubMed:9282742, PubMed:9495771, PubMed:9603865, PubMed:9882666, PubMed:10027987, PubMed:24750258). Binds ATP (PubMed:11053380).9 Publications

GO - Molecular functioni

  • ATP binding Source: EcoCyc
  • identical protein binding Source: IntAct

GO - Biological processi

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

Keywords - Biological processi

Cell cycle, Cell division, Cell shape

Enzyme and pathway databases

BioCyciEcoCyc:EG10339-MONOMER.
ECOL316407:JW0092-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsAUniRule annotation
Gene namesi
Name:ftsAUniRule annotation
Synonyms:divA
Ordered Locus Names:b0094, JW0092
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10339. ftsA.

Subcellular locationi

  • Cell inner membrane 2 Publications; Peripheral membrane protein 2 Publications; Cytoplasmic side 2 Publications

  • Note: Localizes to the Z ring in an FtsZ-dependent manner (PubMed:8955398, PubMed:8917533, PubMed:9495771). Targeted to the membrane through a conserved C-terminal amphiphatic helix (PubMed:15752196).4 Publications

GO - Cellular componenti

  • cell division site Source: EcoliWiki
  • cytoplasmic side of plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi210 – 2101D → A: Does not bind ATP. 1 Publication
Mutagenesisi408 – 4081W → E: Prevents localization to the Z ring. Lack of activity. 1 Publication
Mutagenesisi409 – 4091I → E: Prevents localization to the Z ring. Lack of activity. 1 Publication
Mutagenesisi411 – 4111R → E: Does not affect localization or function. 1 Publication
Mutagenesisi412 – 4121L → E: Prevents localization to the Z ring. Lack of activity. 1 Publication
Mutagenesisi415 – 4151W → E: Prevents localization to the Z ring. Lack of activity. 1 Publication
Mutagenesisi416 – 4161L → E: Prevents localization to the Z ring. Lack of activity. 1 Publication
Mutagenesisi420 – 4201F → E: Does not affect localization or function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420Cell division protein FtsAPRO_0000062734Add
BLAST

Proteomic databases

PaxDbiP0ABH0.
PRIDEiP0ABH0.

Interactioni

Subunit structurei

Self-interacts (PubMed:11053380, PubMed:17501933). Interacts with FtsZ. This interaction plays an essential role in cell division (PubMed:8917533, PubMed:17501933). Interacts directly with the cytoplasmic region of FtsN (PubMed:22328664, PubMed:24750258).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-550562,EBI-550562
ftsNP291317EBI-550562,EBI-1134233
ftsZP0A9A66EBI-550562,EBI-370963

Protein-protein interaction databases

DIPiDIP-47983N.
IntActiP0ABH0. 26 interactions.
STRINGi511145.b0094.

Structurei

3D structure databases

ProteinModelPortaliP0ABH0.
SMRiP0ABH0. Positions 11-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The extreme C-terminus is essential for localization to the membrane and the Z ring, self-interaction and activity.2 Publications

Sequence similaritiesi

Belongs to the FtsA/MreB family.UniRule annotationCurated

Phylogenomic databases

eggNOGiCOG0849.
HOGENOMiHOG000049205.
InParanoidiP0ABH0.
KOiK03590.
OMAiHTAVIPF.
OrthoDBiEOG6TR0B6.
PhylomeDBiP0ABH0.

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.

P0ABH0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKATDRKLV VGLEIGTAKV AALVGEVLPD GMVNIIGVGS CPSRGMDKGG
60 70 80 90 100
VNDLESVVKC VQRAIDQAEL MADCQISSVY LALSGKHISC QNEIGMVPIS
110 120 130 140 150
EEEVTQEDVE NVVHTAKSVR VRDEHRVLHV IPQEYAIDYQ EGIKNPVGLS
160 170 180 190 200
GVRMQAKVHL ITCHNDMAKN IVKAVERCGL KVDQLIFAGL ASSYSVLTED
210 220 230 240 250
ERELGVCVVD IGGGTMDIAV YTGGALRHTK VIPYAGNVVT SDIAYAFGTP
260 270 280 290 300
PSDAEAIKVR HGCALGSIVG KDESVEVPSV GGRPPRSLQR QTLAEVIEPR
310 320 330 340 350
YTELLNLVNE EILQLQEKLR QQGVKHHLAA GIVLTGGAAQ IEGLAACAQR
360 370 380 390 400
VFHTQVRIGA PLNITGLTDY AQEPYYSTAV GLLHYGKESH LNGEAEVEKR
410 420
VTASVGSWIK RLNSWLRKEF
Length:420
Mass (Da):45,330
Last modified:January 1, 1988 - v1
Checksum:iC2475377A229B982
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti339 – 3391A → R (PubMed:6094474).Curated
Sequence conflicti339 – 3391A → R (PubMed:2846985).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02668 Genomic DNA. Translation: AAA23817.1.
M36531 Genomic DNA. Translation: AAA23811.1.
X55034 Genomic DNA. Translation: CAA38871.1.
U00096 Genomic DNA. Translation: AAC73205.1.
AP009048 Genomic DNA. Translation: BAB96662.1.
PIRiB23318. CEECA.
RefSeqiNP_414636.1. NC_000913.3.
WP_000588474.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC73205; AAC73205; b0094.
BAB96662; BAB96662; BAB96662.
GeneIDi944778.
KEGGieco:b0094.
PATRICi32115293. VBIEscCol129921_0098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02668 Genomic DNA. Translation: AAA23817.1.
M36531 Genomic DNA. Translation: AAA23811.1.
X55034 Genomic DNA. Translation: CAA38871.1.
U00096 Genomic DNA. Translation: AAC73205.1.
AP009048 Genomic DNA. Translation: BAB96662.1.
PIRiB23318. CEECA.
RefSeqiNP_414636.1. NC_000913.3.
WP_000588474.1. NZ_CP010445.1.

3D structure databases

ProteinModelPortaliP0ABH0.
SMRiP0ABH0. Positions 11-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47983N.
IntActiP0ABH0. 26 interactions.
STRINGi511145.b0094.

Proteomic databases

PaxDbiP0ABH0.
PRIDEiP0ABH0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73205; AAC73205; b0094.
BAB96662; BAB96662; BAB96662.
GeneIDi944778.
KEGGieco:b0094.
PATRICi32115293. VBIEscCol129921_0098.

Organism-specific databases

EchoBASEiEB0335.
EcoGeneiEG10339. ftsA.

Phylogenomic databases

eggNOGiCOG0849.
HOGENOMiHOG000049205.
InParanoidiP0ABH0.
KOiK03590.
OMAiHTAVIPF.
OrthoDBiEOG6TR0B6.
PhylomeDBiP0ABH0.

Enzyme and pathway databases

BioCyciEcoCyc:EG10339-MONOMER.
ECOL316407:JW0092-MONOMER.

Miscellaneous databases

PROiP0ABH0.

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. "DNA sequence and transcriptional organization of essential cell division genes ftsQ and ftsA of Escherichia coli: evidence for overlapping transcriptional units."
    Robinson A.C., Kenan D.J., Hatfull G.F., Sullivan N.F., Spiegelberg R., Donachie W.D.
    J. Bacteriol. 160:546-555(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Structure and expression of the cell division genes ftsQ, ftsA and ftsZ."
    Yi Q.-M., Rockenbach S., Ward J.E. Jr., Lutkenhaus J.
    J. Mol. Biol. 184:399-412(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Mapping and characterization of mutants of the Escherichia coli cell division gene, ftsA."
    Robinson A.C., Begg K.J., Sweeney J., Condie A., Donachie W.D.
    Mol. Microbiol. 2:581-588(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS TEMPERATURE-SENSITIVE.
  4. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Regulation of expression of the ftsA cell division gene by sequences in upstream genes."
    Dewar S.J., Donachie W.D.
    J. Bacteriol. 172:6611-6614(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
  8. "The nucleotide sequence of the essential cell-division gene ftsZ of Escherichia coli."
    Yi Q.-M., Lutkenhaus J.
    Gene 36:241-247(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 318-420.
    Strain: K12.
  9. "The native form of FtsA, a septal protein of Escherichia coli, is located in the cytoplasmic membrane."
    Pla J., Dopazo A., Vicente M.
    J. Bacteriol. 172:5097-5102(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / ATCC 35607 / JM83.
  10. "FtsA is localized to the septum in an FtsZ-dependent manner."
    Addinall S.G., Lutkenhaus J.
    J. Bacteriol. 178:7167-7172(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12.
  11. "Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein."
    Ma X., Ehrhardt D.W., Margolin W.
    Proc. Natl. Acad. Sci. U.S.A. 93:12998-13003(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FTSZ.
  12. "FtsN, a late recruit to the septum in Escherichia coli."
    Addinall S.G., Cao C., Lutkenhaus J.
    Mol. Microbiol. 25:303-309(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECRUITMENT OF FTSN.
    Strain: K12.
  13. "Localization of cell division protein FtsK to the Escherichia coli septum and identification of a potential N-terminal targeting domain."
    Yu X.C., Tran A.H., Sun Q., Margolin W.
    J. Bacteriol. 180:1296-1304(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECRUITMENT OF FTSK, SUBCELLULAR LOCATION.
  14. "FtsI and FtsW are localized to the septum in Escherichia coli."
    Wang L., Khattar M.K., Donachie W.D., Lutkenhaus J.
    J. Bacteriol. 180:2810-2816(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECRUITMENT OF FTSI.
  15. "Septal localization of FtsQ, an essential cell division protein in Escherichia coli."
    Chen J.C., Weiss D.S., Ghigo J.M., Beckwith J.
    J. Bacteriol. 181:521-530(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECRUITMENT OF FTSQ.
  16. "Localization of FtsL to the Escherichia coli septal ring."
    Ghigo J.M., Weiss D.S., Chen J.C., Yarrow J.C., Beckwith J.
    Mol. Microbiol. 31:725-737(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECRUITMENT OF FTSL.
  17. "Role of the carboxy terminus of Escherichia coli FtsA in self-interaction and cell division."
    Yim L., Vandenbussche G., Mingorance J., Rueda S., Casanova M., Ruysschaert J.M., Vicente M.
    J. Bacteriol. 182:6366-6373(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ATP-BINDING, SUBUNIT, DOMAIN, MUTAGENESIS OF ASP-210.
  18. "Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli."
    Pichoff S., Lutkenhaus J.
    EMBO J. 21:685-693(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA."
    Pichoff S., Lutkenhaus J.
    Mol. Microbiol. 55:1722-1734(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF TRP-408; ILE-409; ARG-411; LEU-412; TRP-415; LEU-416 AND PHE-420.
    Strain: K12.
  20. "Identification of a region of FtsA required for interaction with FtsZ."
    Pichoff S., Lutkenhaus J.
    Mol. Microbiol. 64:1129-1138(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSZ AND SELF-INTERACTION.
  21. "The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN."
    Busiek K.K., Eraso J.M., Wang Y., Margolin W.
    J. Bacteriol. 194:1989-2000(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSN.
  22. "A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN."
    Busiek K.K., Margolin W.
    Mol. Microbiol. 92:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECRUITMENT OF FTSN, INTERACTION WITH FTSN.

Entry informationi

Entry nameiFTSA_ECOLI
AccessioniPrimary (citable) accession number: P0ABH0
Secondary accession number(s): P06137, Q47229
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 22, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.