NIKR_HELPY
ID NIKR_HELPY Reviewed; 148 AA.
AC O25896;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Putative nickel-responsive regulator {ECO:0000255|HAMAP-Rule:MF_00476};
GN OrderedLocusNames=HP_1338;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
CC -!- FUNCTION: Transcriptional regulator. {ECO:0000255|HAMAP-Rule:MF_00476}.
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00476};
CC Note=Binds 1 nickel ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00476};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00476}.
CC -!- INTERACTION:
CC O25896; O25896: HP_1338; NbExp=4; IntAct=EBI-528005, EBI-528005;
CC -!- SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family.
CC {ECO:0000255|HAMAP-Rule:MF_00476}.
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DR EMBL; AE000511; AAD08380.1; -; Genomic_DNA.
DR PIR; B64687; B64687.
DR RefSeq; NP_208130.1; NC_000915.1.
DR RefSeq; WP_000380787.1; NC_018939.1.
DR PDB; 2CA9; X-ray; 2.05 A; A/B=1-148.
DR PDB; 2CAD; X-ray; 2.30 A; A/B=1-148.
DR PDB; 2CAJ; X-ray; 2.35 A; A/B=1-148.
DR PDB; 2WVB; X-ray; 1.90 A; A/B=1-148.
DR PDB; 2WVC; X-ray; 2.10 A; A/B=1-148.
DR PDB; 2WVD; X-ray; 2.65 A; A/B/C/D=1-148.
DR PDB; 2WVE; X-ray; 2.30 A; A/B=1-148.
DR PDB; 2WVF; X-ray; 1.60 A; A/B=1-148.
DR PDB; 3LGH; X-ray; 2.37 A; A/B/C/D=1-148.
DR PDB; 3PHT; X-ray; 2.04 A; A/B=1-148.
DR PDB; 3QSI; X-ray; 3.08 A; A/B/C/D/E/F/G/H/I/J=61-148.
DR PDB; 6MRJ; X-ray; 2.80 A; A/B/C/D=1-148.
DR PDBsum; 2CA9; -.
DR PDBsum; 2CAD; -.
DR PDBsum; 2CAJ; -.
DR PDBsum; 2WVB; -.
DR PDBsum; 2WVC; -.
DR PDBsum; 2WVD; -.
DR PDBsum; 2WVE; -.
DR PDBsum; 2WVF; -.
DR PDBsum; 3LGH; -.
DR PDBsum; 3PHT; -.
DR PDBsum; 3QSI; -.
DR PDBsum; 6MRJ; -.
DR AlphaFoldDB; O25896; -.
DR BMRB; O25896; -.
DR SMR; O25896; -.
DR DIP; DIP-3711N; -.
DR IntAct; O25896; 3.
DR MINT; O25896; -.
DR STRING; 85962.C694_06905; -.
DR PaxDb; O25896; -.
DR EnsemblBacteria; AAD08380; AAD08380; HP_1338.
DR KEGG; hpy:HP_1338; -.
DR PATRIC; fig|85962.47.peg.1433; -.
DR eggNOG; COG0864; Bacteria.
DR OMA; AHNCLET; -.
DR PhylomeDB; O25896; -.
DR EvolutionaryTrace; O25896; -.
DR Proteomes; UP000000429; Chromosome.
DR CollecTF; EXPREG_00000670; -.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CollecTF.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0010045; P:response to nickel cation; IEA:InterPro.
DR Gene3D; 1.10.1220.10; -; 1.
DR Gene3D; 3.30.70.1150; -; 1.
DR HAMAP; MF_00476; NikR; 1.
DR InterPro; IPR027271; Acetolactate_synth/TF_NikR_C.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR InterPro; IPR002145; CopG.
DR InterPro; IPR022988; Ni_resp_reg_NikR.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
DR InterPro; IPR014864; TF_NikR_Ni-bd_C.
DR Pfam; PF08753; NikR_C; 1.
DR Pfam; PF01402; RHH_1; 1.
DR SUPFAM; SSF47598; SSF47598; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Nickel; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..148
FT /note="Putative nickel-responsive regulator"
FT /id="PRO_0000139291"
FT BINDING 88
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00476"
FT BINDING 99
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00476"
FT BINDING 101
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00476"
FT BINDING 107
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00476"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:2WVF"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:2WVF"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:2WVF"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:2CA9"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:2WVF"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3QSI"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:2WVF"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:2WVF"
FT STRAND 103..115
FT /evidence="ECO:0007829|PDB:2WVF"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:2WVF"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:2WVF"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2WVF"
SQ SEQUENCE 148 AA; 17147 MW; 9C8A2F803E7822B8 CRC64;
MDTPNKDDSI IRFSVSLQQN LLDELDNRII KNGYSSRSEL VRDMIREKLV EDNWAEDNPN
DESKIAVLVV IYDHHQRELN QRMIDIQHAS GTHVLCTTHI HMDEHNCLET IILQGNSFEI
QRLQLEIGGL RGVKFAKLTK ASSFEYNE
