ID   FITA_NEIG1              Reviewed;          78 AA.
AC   Q5F881; Q9RF92;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Antitoxin FitA;
DE   AltName: Full=Trafficking protein A;
GN   Name=fitA; Synonyms=vapB; OrderedLocusNames=NGO0908;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700825 / FA 1090, and MS11A;
RX   PubMed=10639460; DOI=10.1128/iai.68.2.896-905.2000;
RA   Hopper S., Wilbur J.S., Vasquez B.L., Larson J., Clary S., Mehr I.J.,
RA   Seifert H.S., So M.;
RT   "Isolation of Neisseria gonorrhoeae mutants that show enhanced trafficking
RT   across polarized T84 epithelial monolayers.";
RL   Infect. Immun. 68:896-905(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   DNA-BINDING, SUBUNIT, AND MUTAGENESIS OF ARG-7.
RC   STRAIN=ATCC 700825 / FA 1090;
RX   PubMed=16156663; DOI=10.1021/bi0511080;
RA   Wilbur J.S., Chivers P.T., Mattison K., Potter L., Brennan R.G., So M.;
RT   "Neisseria gonorrhoeae FitA interacts with FitB to bind DNA through its
RT   ribbon-helix-helix motif.";
RL   Biochemistry 44:12515-12524(2005).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-78 IN COMPLEX WITH FITB BOUND
RP   TO DNA, SUBUNIT, AND DNA-BINDING.
RC   STRAIN=ATCC 700825 / FA 1090;
RX   PubMed=16982615; DOI=10.1074/jbc.m605198200;
RA   Mattison K., Wilbur J.S., So M., Brennan R.G.;
RT   "Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a
RT   tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-
RT   helix-helix motifs.";
RL   J. Biol. Chem. 281:37942-37951(2006).
CC   -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC       Plays a role in the speed with which bacteria traverse human epithelial
CC       cells; disruption of the locus increases the speed of trafficking about
CC       2-4-fold. Binds to its own promoter, binding affinity of the FitAB
CC       complex is 20-30-fold higher than FitA alone. No nuclease activity was
CC       observed for the FitAB complex, perhaps because FitA (the antitoxin)
CC       prevents metal binding and thus catalysis by FitB.
CC       {ECO:0000269|PubMed:10639460}.
CC   -!- SUBUNIT: Homodimer in the absence of FitB; forms a heterodimer with
CC       FitB; 4 FitAB heterodimers form a complex that binds to fitAB promoter
CC       DNA. The complex is also seen in solution.
CC       {ECO:0000269|PubMed:16156663, ECO:0000269|PubMed:16982615}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the fitAB operon leads to faster
CC       transepithelial cell trafficking of the bacterium; mutants adhere to
CC       and invade cells normally. Mutants grow normally in liquid culture but
CC       much faster within human cell lines A431 and T84; these latter 2
CC       phenotypes were observed using MS11A bacteria with a disrupted fitAB
CC       locus. {ECO:0000269|PubMed:10639460}.
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DR   EMBL; AF200716; AAF19188.1; -; Genomic_DNA.
DR   EMBL; AE004969; AAW89606.1; -; Genomic_DNA.
DR   RefSeq; WP_003688410.1; NC_002946.2.
DR   RefSeq; YP_208018.1; NC_002946.2.
DR   PDB; 2BSQ; X-ray; 3.00 A; E/F/G/H=2-78.
DR   PDB; 2H1C; X-ray; 1.80 A; B=46-64.
DR   PDB; 2H1O; X-ray; 3.00 A; E/F/G/H=2-69.
DR   PDBsum; 2BSQ; -.
DR   PDBsum; 2H1C; -.
DR   PDBsum; 2H1O; -.
DR   AlphaFoldDB; Q5F881; -.
DR   SMR; Q5F881; -.
DR   EnsemblBacteria; AAW89606; AAW89606; NGO_0908.
DR   GeneID; 66753237; -.
DR   KEGG; ngo:NGO_0908; -.
DR   PATRIC; fig|242231.10.peg.1068; -.
DR   HOGENOM; CLU_168829_4_0_4; -.
DR   OMA; CIMPVIT; -.
DR   EvolutionaryTrace; Q5F881; -.
DR   Proteomes; UP000000535; Chromosome.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0044001; P:migration in host; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.1220.10; -; 1.
DR   InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR   InterPro; IPR010985; Ribbon_hlx_hlx.
DR   SUPFAM; SSF47598; SSF47598; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Toxin-antitoxin system.
FT   CHAIN           1..78
FT                   /note="Antitoxin FitA"
FT                   /id="PRO_0000408086"
FT   MUTAGEN         7
FT                   /note="R->A: Loss of DNA-binding, still binds FitB."
FT                   /evidence="ECO:0000269|PubMed:16156663"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:2BSQ"
FT   HELIX           11..23
FT                   /evidence="ECO:0007829|PDB:2BSQ"
FT   HELIX           28..43
FT                   /evidence="ECO:0007829|PDB:2BSQ"
FT   HELIX           48..59
FT                   /evidence="ECO:0007829|PDB:2H1C"
SQ   SEQUENCE   78 AA;  8434 MW;  29CC28FF3DCD9C73 CRC64;
     MASVVIRNLS EATHNAIKFR ARAAGRSTEA EIRLILDNIA KAQQTVRLGS MLASIGQEIG
     GVELEDVRGR NTDNEVSL