GCH1L_ECOLI
ID GCH1L_ECOLI Reviewed; 247 AA.
AC P0AFP6; P75743;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog {ECO:0000305};
DE AltName: Full=Radiation resistance protein YbgI {ECO:0000303|PubMed:25049088};
GN Name=ybgI; OrderedLocusNames=b0710, JW0700;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=25049088; DOI=10.1128/jb.01589-14;
RA Byrne R.T., Chen S.H., Wood E.A., Cabot E.L., Cox M.M.;
RT "Escherichia coli genes and pathways involved in surviving extreme exposure
RT to ionizing radiation.";
RL J. Bacteriol. 196:3534-3545(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH METAL IONS, AND
RP SUBUNIT.
RX PubMed=14519207; DOI=10.1186/1472-6807-3-7;
RA Ladner J.E., Obmolova G., Teplyakov A., Howard A.J., Khil P.P.,
RA Camerini-Otero R.D., Gilliland G.L.;
RT "Crystal structure of Escherichia coli protein ybgI, a toroidal structure
RT with a dinuclear metal site.";
RL BMC Struct. Biol. 3:7-7(2003).
CC -!- FUNCTION: Provides significant protection from radiation damage and may
CC be involved in the degradation of radiation-damaged nucleotides.
CC {ECO:0000269|PubMed:25049088}.
CC -!- SUBUNIT: Toroid-shaped homohexamer. In the hexamer, 3 dimers assemble
CC to form a ring-like structure surrounding a central hole.
CC {ECO:0000269|PubMed:14519207}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a 2-3 orders of
CC magnitude drop in survival after exposure to ionizing radiation as
CC compared to a wild-type strain. {ECO:0000269|PubMed:25049088}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC73804.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35374.1; -; Genomic_DNA.
DR PIR; E64806; E64806.
DR RefSeq; NP_415238.1; NC_000913.3.
DR RefSeq; WP_000798871.1; NZ_STEB01000035.1.
DR PDB; 1NMO; X-ray; 2.20 A; A/B/C/D/E/F=1-247.
DR PDB; 1NMP; X-ray; 2.20 A; A/B/C/D/E/F=1-247.
DR PDBsum; 1NMO; -.
DR PDBsum; 1NMP; -.
DR AlphaFoldDB; P0AFP6; -.
DR SMR; P0AFP6; -.
DR BioGRID; 4259921; 139.
DR DIP; DIP-36185N; -.
DR IntAct; P0AFP6; 6.
DR STRING; 511145.b0710; -.
DR jPOST; P0AFP6; -.
DR PaxDb; P0AFP6; -.
DR PRIDE; P0AFP6; -.
DR EnsemblBacteria; AAC73804; AAC73804; b0710.
DR EnsemblBacteria; BAA35374; BAA35374; BAA35374.
DR GeneID; 66671021; -.
DR GeneID; 945824; -.
DR KEGG; ecj:JW0700; -.
DR KEGG; eco:b0710; -.
DR PATRIC; fig|1411691.4.peg.1563; -.
DR EchoBASE; EB3089; -.
DR eggNOG; COG0327; Bacteria.
DR HOGENOM; CLU_037423_3_0_6; -.
DR InParanoid; P0AFP6; -.
DR OMA; HGLFWRG; -.
DR PhylomeDB; P0AFP6; -.
DR BioCyc; EcoCyc:G6379-MON; -.
DR EvolutionaryTrace; P0AFP6; -.
DR PRO; PR:P0AFP6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0060187; C:cell pole; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034214; P:protein hexamerization; IDA:EcoCyc.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:EcoCyc.
DR InterPro; IPR002678; DUF34/NIF3.
DR InterPro; IPR036069; DUF34/NIF3_sf.
DR PANTHER; PTHR13799; PTHR13799; 1.
DR Pfam; PF01784; NIF3; 1.
DR SUPFAM; SSF102705; SSF102705; 1.
DR TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Metal-binding; Reference proteome.
FT CHAIN 1..247
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147307"
FT BINDING 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:14519207"
FT BINDING 64
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14519207"
FT BINDING 101
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:14519207"
FT BINDING 215
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14519207"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:14519207"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14519207"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:1NMO"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:1NMO"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:1NMO"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1NMO"
SQ SEQUENCE 247 AA; 26892 MW; 07436A9E410DF007 CRC64;
MKNTELEQLI NEKLNSAAIS DYAPNGLQVE GKETVQKIVT GVTASQALLD EAVRLGADAV
IVHHGYFWKG ESPVIRGMKR NRLKTLLAND INLYGWHLPL DAHPELGNNA QLAALLGITV
MGEIEPLVPW GELTMPVPGL ELASWIEARL GRKPLWCGDT GPEVVQRVAW CTGGGQSFID
SAARFGVDAF ITGEVSEQTI HSAREQGLHF YAAGHHATER GGIRALSEWL NENTDLDVTF
IDIPNPA
