YJIA_ECOLI
ID YJIA_ECOLI Reviewed; 318 AA.
AC P24203; Q2M5W4;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=P-loop guanosine triphosphatase YjiA {ECO:0000303|PubMed:14696199};
DE EC=3.6.-.- {ECO:0000269|PubMed:14696199, ECO:0000269|PubMed:24449932};
DE AltName: Full=GTP-binding protein YjiA {ECO:0000305};
GN Name=yjiA; OrderedLocusNames=b4352, JW5790;
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 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-318.
RC STRAIN=K12;
RX PubMed=1650347; DOI=10.1128/jb.173.16.5207-5219.1991;
RA Waite-Rees P.A., Keating C.J., Moran L.S., Slatko B.E., Hornstra L.J.,
RA Benner J.S.;
RT "Characterization and expression of the Escherichia coli Mrr restriction
RT system.";
RL J. Bacteriol. 173:5207-5219(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, AND GTP-BINDING.
RX PubMed=14696199; DOI=10.1002/prot.10430;
RA Khil P.P., Obmolova G., Teplyakov A., Howard A.J., Gilliland G.L.,
RA Camerini-Otero R.D.;
RT "Crystal structure of the Escherichia coli YjiA protein suggests a GTP-
RT dependent regulatory function.";
RL Proteins 54:371-374(2004).
RN [6] {ECO:0007744|PDB:4IXM, ECO:0007744|PDB:4IXN}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=24449932; DOI=10.1021/bi301600z;
RA Sydor A.M., Jost M., Ryan K.S., Turo K.E., Douglas C.D., Drennan C.L.,
RA Zamble D.B.;
RT "Metal binding properties of Escherichia coli YjiA, a member of the metal
RT homeostasis-associated COG0523 family of GTPases.";
RL Biochemistry 52:1788-1801(2013).
CC -!- FUNCTION: Binds GTP and has low GTPase activity. May have a GTP-
CC dependent regulatory function. {ECO:0000269|PubMed:14696199,
CC ECO:0000269|PubMed:24449932}.
CC -!- ACTIVITY REGULATION: GTPase activity is inhibited by metal binding.
CC Activity is decreased in the presence of Co(II) or Ni(II), and is
CC completely inhibited in the presence of Zn(II).
CC {ECO:0000269|PubMed:24449932}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.006 sec(-1) for GTP hydrolysis in the absence of
CC metal. kcat is 0.0005 sec(-1) for GTP hydrolysis in the presence of
CC Co(II). {ECO:0000269|PubMed:24449932};
CC -!- SUBUNIT: Monomer in the apo form. Metal binding induces
CC oligomerization. Forms homodimers and higher oligomers.
CC {ECO:0000269|PubMed:24449932}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. CobW
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97249.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97249.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC77308.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78342.1; -; Genomic_DNA.
DR EMBL; X54198; CAA38118.1; -; Genomic_DNA.
DR PIR; S56578; S56578.
DR RefSeq; NP_418772.4; NC_000913.3.
DR RefSeq; WP_001312515.1; NZ_LN832404.1.
DR PDB; 1NIJ; X-ray; 2.00 A; A=1-318.
DR PDB; 4IXM; X-ray; 2.57 A; A/B=1-318.
DR PDB; 4IXN; X-ray; 2.05 A; A/B=1-318.
DR PDBsum; 1NIJ; -.
DR PDBsum; 4IXM; -.
DR PDBsum; 4IXN; -.
DR AlphaFoldDB; P24203; -.
DR SMR; P24203; -.
DR BioGRID; 4262771; 37.
DR BioGRID; 853160; 1.
DR DIP; DIP-12630N; -.
DR IntAct; P24203; 2.
DR STRING; 511145.b4352; -.
DR jPOST; P24203; -.
DR PaxDb; P24203; -.
DR PRIDE; P24203; -.
DR EnsemblBacteria; AAC77308; AAC77308; b4352.
DR EnsemblBacteria; BAE78342; BAE78342; BAE78342.
DR GeneID; 948882; -.
DR KEGG; ecj:JW5790; -.
DR KEGG; eco:b4352; -.
DR PATRIC; fig|1411691.4.peg.2334; -.
DR EchoBASE; EB0020; -.
DR eggNOG; COG0523; Bacteria.
DR HOGENOM; CLU_017452_0_2_6; -.
DR InParanoid; P24203; -.
DR OMA; MWGVLRY; -.
DR PhylomeDB; P24203; -.
DR BioCyc; EcoCyc:EG10021-MON; -.
DR BioCyc; MetaCyc:EG10021-MON; -.
DR EvolutionaryTrace; P24203; -.
DR PRO; PR:P24203; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046914; F:transition metal ion binding; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR Gene3D; 3.30.1220.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011629; Cbl_biosynth_CobW-like_C.
DR InterPro; IPR036627; CobW-likC_sf.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SMART; SM00833; CobW_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..318
FT /note="P-loop guanosine triphosphatase YjiA"
FT /evidence="ECO:0000255"
FT /id="PRO_0000169785"
FT DOMAIN 224..315
FT /note="CobW C-terminal"
FT /evidence="ECO:0000255"
FT BINDING 11..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P9WPZ1"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P9WPZ1"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:24449932"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:24449932"
FT STRAND 4..16
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:1NIJ"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1NIJ"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4IXM"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:1NIJ"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:1NIJ"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:1NIJ"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:1NIJ"
SQ SEQUENCE 318 AA; 35660 MW; 6D68463182031C41 CRC64;
MNPIAVTLLT GFLGAGKTTL LRHILNEQHG YKIAVIENEF GEVSVDDQLI GDRATQIKTL
TNGCICCSRS NELEDALLDL LDNLDKGNIQ FDRLVIECTG MADPGPIIQT FFSHEVLCQR
YLLDGVIALV DAVHADEQMN QFTIAQSQVG YADRILLTKT DVAGEAEKLH ERLARINARA
PVYTVTHGDI DLGLLFNTNG FMLEENVVST KPRFHFIADK QNDISSIVVE LDYPVDISEV
SRVMENLLLE SADKLLRYKG MLWIDGEPNR LLFQGVQRLY SADWDRPWGD EKPHSTMVFI
GIQLPEEEIR AAFAGLRK
