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

Antitoxin FitA

Gene

fitA

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Antitoxin component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. Binds to its own promoter, binding affinity of the FitAB complex is 20-30-fold higher than FitA alone. No nuclease activity was observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • migration in host Source: UniProtKB
  • regulation of transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciNGON242231:GI2G-848-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Antitoxin FitA
Alternative name(s):
Trafficking protein A
Gene namesi
Name:fitA
Synonyms:vapB
Ordered Locus Names:NGO0908
OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Taxonomic identifieri242231 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000000535 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Disruption of the fitAB operon leads to faster transepithelial cell trafficking of the bacterium; mutants adhere to and invade cells normally. Mutants grow normally in liquid culture but much faster within human cell lines A431 and T84; these latter 2 phenotypes were observed using MS11A bacteria with a disrupted fitAB locus.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71R → A: Loss of DNA-binding, still binds FitB. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7878Antitoxin FitAPRO_0000408086Add
BLAST

Interactioni

Subunit structurei

Homodimer in the absence of FitB; forms a heterodimer with FitB; 4 FitAB heterodimers form a complex that binds to fitAB promoter DNA. The complex is also seen in solution.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

1
78
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi11 – 2313Combined sources
Helixi28 – 4316Combined sources
Helixi48 – 5912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BSQX-ray3.00E/F/G/H2-78[»]
2H1CX-ray1.80B46-64[»]
2H1OX-ray3.00E/F/G/H2-69[»]
ProteinModelPortaliQ5F881.
SMRiQ5F881. Positions 2-69.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5F881.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000142203.
OMAiCIMPVIT.
OrthoDBiEOG6HQSV9.

Family and domain databases

InterProiIPR010985. Ribbon_hlx_hlx.
[Graphical view]
SUPFAMiSSF47598. SSF47598. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5F881-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVVIRNLS EATHNAIKFR ARAAGRSTEA EIRLILDNIA KAQQTVRLGS
60 70
MLASIGQEIG GVELEDVRGR NTDNEVSL
Length:78
Mass (Da):8,434
Last modified:March 15, 2005 - v1
Checksum:i29CC28FF3DCD9C73
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF200716 Genomic DNA. Translation: AAF19188.1.
AE004969 Genomic DNA. Translation: AAW89606.1.
RefSeqiWP_003688410.1. NC_002946.2.
YP_208018.1. NC_002946.2.

Genome annotation databases

EnsemblBacteriaiAAW89606; AAW89606; NGO_0908.
GeneIDi3281660.
KEGGingo:NGO0908.
PATRICi20334997. VBINeiGon24812_1068.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF200716 Genomic DNA. Translation: AAF19188.1.
AE004969 Genomic DNA. Translation: AAW89606.1.
RefSeqiWP_003688410.1. NC_002946.2.
YP_208018.1. NC_002946.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BSQX-ray3.00E/F/G/H2-78[»]
2H1CX-ray1.80B46-64[»]
2H1OX-ray3.00E/F/G/H2-69[»]
ProteinModelPortaliQ5F881.
SMRiQ5F881. Positions 2-69.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW89606; AAW89606; NGO_0908.
GeneIDi3281660.
KEGGingo:NGO0908.
PATRICi20334997. VBINeiGon24812_1068.

Phylogenomic databases

HOGENOMiHOG000142203.
OMAiCIMPVIT.
OrthoDBiEOG6HQSV9.

Enzyme and pathway databases

BioCyciNGON242231:GI2G-848-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5F881.

Family and domain databases

InterProiIPR010985. Ribbon_hlx_hlx.
[Graphical view]
SUPFAMiSSF47598. SSF47598. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of Neisseria gonorrhoeae mutants that show enhanced trafficking across polarized T84 epithelial monolayers."
    Hopper S., Wilbur J.S., Vasquez B.L., Larson J., Clary S., Mehr I.J., Seifert H.S., So M.
    Infect. Immun. 68:896-905(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE.
    Strain: ATCC 700825 / FA 1090 and MS11A.
  2. "The complete genome sequence of Neisseria gonorrhoeae."
    Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
    , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700825 / FA 1090.
  3. "Neisseria gonorrhoeae FitA interacts with FitB to bind DNA through its ribbon-helix-helix motif."
    Wilbur J.S., Chivers P.T., Mattison K., Potter L., Brennan R.G., So M.
    Biochemistry 44:12515-12524(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, SUBUNIT, MUTAGENESIS OF ARG-7.
    Strain: ATCC 700825 / FA 1090.
  4. "Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifs."
    Mattison K., Wilbur J.S., So M., Brennan R.G.
    J. Biol. Chem. 281:37942-37951(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-78 IN COMPLEX WITH FITB BOUND TO DNA, SUBUNIT, DNA-BINDING.
    Strain: ATCC 700825 / FA 1090.

Entry informationi

Entry nameiFITA_NEIG1
AccessioniPrimary (citable) accession number: Q5F881
Secondary accession number(s): Q9RF92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 15, 2005
Last modified: December 9, 2015
This is version 69 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.