ID   KGUA_RICCN              Reviewed;         229 AA.
AC   Q92GC9;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
GN   Name=gmk; OrderedLocusNames=RC1194;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:456216; EC=2.7.4.8;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR   EMBL; AE006914; AAL03732.1; -; Genomic_DNA.
DR   PIR; B97849; B97849.
DR   RefSeq; WP_010977760.1; NC_003103.1.
DR   AlphaFoldDB; Q92GC9; -.
DR   SMR; Q92GC9; -.
DR   EnsemblBacteria; AAL03732; AAL03732; RC1194.
DR   KEGG; rco:RC1194; -.
DR   HOGENOM; CLU_001715_1_0_5; -.
DR   OMA; EWAVVHG; -.
DR   BRENDA; 2.7.4.8; 5446.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004385; F:guanylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00328; Guanylate_kinase; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR017665; Guanylate_kinase.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005728; Rickett_RPE.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03263; guanyl_kin; 1.
DR   TIGRFAMs; TIGR01045; RPE1; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..229
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170595"
FT   DOMAIN          7..42
FT                   /note="RPE1 insert"
FT   DOMAIN          44..222
FT                   /note="Guanylate kinase-like"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   229 AA;  26188 MW;  E8A00804520C0214 CRC64;
     MTTKNKRVLQ KCAYREEFKG DMERSTAATS KLPLEVELSR NSKGLIIILS SPSGTGKSSL
     AKALLKIDNN LRLSISATTR KPRLGEVEGI NYYFKTGLEF EELVKQNKFL EYAKIYDNYY
     GTPKEYVEML LNQGLDVLFD IDWQGARSIK KNATNVVTIF VLPPNIEVLE QRLRNRATDN
     EEAIKLRMQL AQNEISHANE YDYVVTNDDF DRTLKKIHAI IVAARDKAF