UREG_HELPY
ID UREG_HELPY Reviewed; 199 AA.
AC Q09066;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=HP_0068;
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 [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=85P;
RX PubMed=1313413; DOI=10.1128/jb.174.8.2466-2473.1992;
RA Cussac V., Ferrero R.L., Labigne A.;
RT "Expression of Helicobacter pylori urease genes in Escherichia coli grown
RT under nitrogen-limiting conditions.";
RL J. Bacteriol. 174:2466-2473(1992).
RN [2]
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).
RN [3]
RP MUTAGENESIS OF LYS-14.
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX PubMed=14521881; DOI=10.1016/s0882-4010(03)00151-7;
RA Mehta N., Benoit S., Maier R.J.;
RT "Roles of conserved nucleotide-binding domains in accessory proteins, HypB
RT and UreG, in the maturation of nickel-enzymes required for efficient
RT Helicobacter pylori colonization.";
RL Microb. Pathog. 35:229-234(2003).
RN [4]
RP REVIEW ON VIRULENCE OF H.PYLORI.
RX PubMed=17313591; DOI=10.1111/j.1574-6968.2007.00648.x;
RA Clyne M., Dolan B., Reeves E.P.;
RT "Bacterial factors that mediate colonization of the stomach and virulence
RT of Helicobacter pylori.";
RL FEMS Microbiol. Lett. 268:135-143(2007).
CC -!- FUNCTION: Facilitates the functional incorporation of the urease nickel
CC metallocenter. This process requires GTP hydrolysis, probably
CC effectuated by UreG. {ECO:0000255|HAMAP-Rule:MF_01389}.
CC -!- SUBUNIT: Homodimer. UreH, UreF and UreG form a complex that acts as a
CC GTP-hydrolysis-dependent molecular chaperone, activating the urease
CC apoprotein by helping to assemble the nickel containing metallocenter
CC of UreC. The UreE protein probably delivers the nickel.
CC {ECO:0000255|HAMAP-Rule:MF_01389}.
CC -!- INTERACTION:
CC Q09066; Q09064: ureE; NbExp=3; IntAct=EBI-7742750, EBI-7742396;
CC Q09066; Q09065: ureF; NbExp=6; IntAct=EBI-7742750, EBI-7743673;
CC Q09066; Q09066: ureG; NbExp=3; IntAct=EBI-7742750, EBI-7742750;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01389}.
CC -!- DISRUPTION PHENOTYPE: Cells do not express urease.
CC {ECO:0000269|PubMed:1313413}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01389}.
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DR EMBL; M84338; AAA25025.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07131.1; -; Genomic_DNA.
DR PIR; D64528; D64528.
DR RefSeq; NP_206868.1; NC_000915.1.
DR RefSeq; WP_000238762.1; NC_018939.1.
DR PDB; 4HI0; X-ray; 2.35 A; E/F=1-199.
DR PDBsum; 4HI0; -.
DR AlphaFoldDB; Q09066; -.
DR SMR; Q09066; -.
DR DIP; DIP-3131N; -.
DR IntAct; Q09066; 3.
DR MINT; Q09066; -.
DR STRING; 85962.C694_00325; -.
DR PaxDb; Q09066; -.
DR PRIDE; Q09066; -.
DR DNASU; 899102; -.
DR EnsemblBacteria; AAD07131; AAD07131; HP_0068.
DR GeneID; 66521325; -.
DR KEGG; hpy:HP_0068; -.
DR PATRIC; fig|85962.47.peg.71; -.
DR eggNOG; COG0378; Bacteria.
DR OMA; VDLTIYV; -.
DR PhylomeDB; Q09066; -.
DR BioCyc; MetaCyc:HP_RS00345-MON; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01389; UreG; 1.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004400; UreG.
DR PANTHER; PTHR31715; PTHR31715; 1.
DR Pfam; PF02492; cobW; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00101; ureG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; GTP-binding; Nickel insertion;
KW Nucleotide-binding; Reference proteome; Virulence.
FT CHAIN 1..199
FT /note="Urease accessory protein UreG"
FT /id="PRO_0000067667"
FT BINDING 8..15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
FT MUTAGEN 14
FT /note="K->A: No urease activity, no effect on hydrogenase
FT activity. Normal amounts of apourease and UreG protein are
FT produced."
FT /evidence="ECO:0000269|PubMed:14521881"
FT CONFLICT 102
FT /note="D -> S (in Ref. 1; AAA25025)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..176
FT /note="MRGEKPFIFT -> IAAKSPLFLP (in Ref. 1; AAA25025)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:4HI0"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:4HI0"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4HI0"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:4HI0"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4HI0"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:4HI0"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:4HI0"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4HI0"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:4HI0"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4HI0"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:4HI0"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:4HI0"
SQ SEQUENCE 199 AA; 21955 MW; A23E448EB6A208B1 CRC64;
MVKIGVCGPV GSGKTALIEA LTRHMSKDYD MAVITNDIYT KEDAEFMCKN SVMPRERIIG
VETGGCPHTA IREDASMNLE AVEEMHGRFP NLELLLIESG GDNLSATFNP ELADFTIFVI
DVAEGDKIPR KGGPGITRSD LLVINKIDLA PYVGADLKVM ERDSKKMRGE KPFIFTNIRA
KEGLDDVIAW IKRNALLED
