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   02-SEP-2026, entry version 170.
DE   RecName: Full=Zinc chaperone YjiA {ECO:0000303|PubMed:14696199};
DE            EC=3.6.5.- {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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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), CATALYTIC ACTIVITY, 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, ACTIVITY
RP   REGULATION, CATALYTIC ACTIVITY, 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: Zinc chaperone that directly transfers zinc cofactor to
CC       target proteins, thereby activating them (By similarity). Zinc is
CC       transferred from the CXCC motif in the GTPase domain to the zinc
CC       binding site in target proteins in a process requiring GTP hydrolysis
CC       (By similarity). {ECO:0000250|UniProtKB:Q8VEH6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:14696199, ECO:0000269|PubMed:24449932};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000269|PubMed:14696199, 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 (PubMed:24449932). Metal binding
CC       induces oligomerization. Forms homodimers and higher oligomers
CC       (PubMed:24449932). {ECO:0000269|PubMed:24449932}.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
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_CP010438.1.
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   AlphaFoldDB; P24203; -.
DR   MDRepo; P24203; -.
DR   SMR; P24203; -.
DR   BioGRID; 4262771; 41.
DR   BioGRID; 853160; 1.
DR   DIP; DIP-12630N; -.
DR   FunCoup; P24203; 606.
DR   IntAct; P24203; 2.
DR   STRING; 511145.b4352; -.
DR   jPOST; P24203; -.
DR   PaxDb; 511145-b4352; -.
DR   EnsemblBacteria; AAC77308; AAC77308; b4352.
DR   GeneID; 948882; -.
DR   KEGG; ecj:JW5790; -.
DR   KEGG; eco:b4352; -.
DR   KEGG; ecoc:C3026_23510; -.
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; HSQGFET; -.
DR   OrthoDB; 9808822at2; -.
DR   PhylomeDB; P24203; -.
DR   BioCyc; EcoCyc:EG10021-MONOMER; -.
DR   BioCyc; MetaCyc:EG10021-MONOMER; -.
DR   EvolutionaryTrace; P24203; -.
DR   PRO; PR:P24203; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P24203; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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:0140827; F:zinc chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR   CDD; cd03112; CobW-like; 1.
DR   FunFam; 3.30.1220.10:FF:000001; GTP-binding protein YjiA; 1.
DR   FunFam; 3.40.50.300:FF:000778; GTP-binding protein YjiA; 1.
DR   Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036627; CobW-likC_sf.
DR   InterPro; IPR011629; CobW-like_C.
DR   InterPro; IPR003495; CobW/HypB/UreG_nucleotide-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR051316; Zinc-reg_GTPase_activator.
DR   NCBIfam; NF008578; PRK11537.1; 1.
DR   PANTHER; PTHR13748:SF62; COBW DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13748; COBW-RELATED; 1.
DR   Pfam; PF02492; cobW; 1.
DR   Pfam; PF07683; CobW_C; 1.
DR   SMART; SM00833; CobW_C; 1.
DR   SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PDBsum; 1NIJ; -.
DR   PDBsum; 4IXM; -.
DR   PDBsum; 4IXN; -.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; GTP-binding; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN           1..318
FT                   /note="Zinc chaperone YjiA"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000169785"
FT   DOMAIN          224..315
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           64..67
FT                   /note="CXCC motif"
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..86
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   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:4IXN"
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
//