FITB_NEIG1
ID FITB_NEIG1 Reviewed; 139 AA.
AC Q5F882; Q9RF91;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Toxin FitB;
DE AltName: Full=Ribonuclease FitB;
DE Short=RNase FitB;
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Trafficking protein B;
GN Name=fitB; Synonyms=vapC; OrderedLocusNames=NGO0907;
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], 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, AND SUBUNIT.
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 1-138 IN COMPLEX WITH FITA BOUND
RP TO DNA, AND SUBUNIT.
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: Toxic 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. FitAB binds to its own promoter better than FitA alone. The
CC expected nuclease activity was not observed for the FitAB complex,
CC perhaps because FitA (the antitoxin) prevents metal binding and thus
CC catalysis by FitB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC -!- SUBUNIT: Forms a heterodimer with FitA, 4 FitAB heterodimers form a
CC complex that binds to promoter DNA. The complex is also seen in
CC solution. This protein does not actually contact DNA.
CC {ECO:0000269|PubMed:16156663, ECO:0000269|PubMed:16982615}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the fitAB locus 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}.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR EMBL; AF200716; AAF19189.1; -; Genomic_DNA.
DR EMBL; AE004969; AAW89605.1; -; Genomic_DNA.
DR RefSeq; WP_003691083.1; NC_002946.2.
DR RefSeq; YP_208017.1; NC_002946.2.
DR PDB; 2BSQ; X-ray; 3.00 A; A/B/C/D=1-139.
DR PDB; 2H1C; X-ray; 1.80 A; A=1-138.
DR PDB; 2H1O; X-ray; 3.00 A; A/B/C/D=1-138.
DR PDBsum; 2BSQ; -.
DR PDBsum; 2H1C; -.
DR PDBsum; 2H1O; -.
DR AlphaFoldDB; Q5F882; -.
DR SMR; Q5F882; -.
DR STRING; 242231.NGO_0907; -.
DR EnsemblBacteria; AAW89605; AAW89605; NGO_0907.
DR GeneID; 66753236; -.
DR KEGG; ngo:NGO_0907; -.
DR PATRIC; fig|242231.10.peg.1067; -.
DR HOGENOM; CLU_118482_8_2_4; -.
DR OMA; VINPWEA; -.
DR EvolutionaryTrace; Q5F882; -.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0044001; P:migration in host; IMP:UniProtKB.
DR HAMAP; MF_00265; VapC_Nob1; 1.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR022907; VapC_family.
DR Pfam; PF01850; PIN; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..139
FT /note="Toxin FitB"
FT /id="PRO_0000407900"
FT DOMAIN 2..123
FT /note="PINc"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2H1C"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2H1C"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:2H1C"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:2H1C"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2H1C"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:2H1C"
SQ SEQUENCE 139 AA; 15307 MW; AE12B8DF0E8427F4 CRC64;
MILLDTNVIS EPLRPQPNER VVAWLDSLIL EDVYLSAITV AELRLGVALL LNGKKKNVLH
ERLEQSILPL FAGRILPFDE PVAAIYAQIR SYAKTHGKEI AAADGYIAAT AKQHSLTVAT
RDTGSFFAAD VAVFNPWHD
