ID   KGUA_EHRRG              Reviewed;         209 AA.
AC   Q5FFZ9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Guanylate kinase {ECO:0000255|HAMAP-Rule:MF_00328};
DE            EC=2.7.4.8 {ECO:0000255|HAMAP-Rule:MF_00328};
DE   AltName: Full=GMP kinase {ECO:0000255|HAMAP-Rule:MF_00328};
GN   Name=gmk {ECO:0000255|HAMAP-Rule:MF_00328};
GN   OrderedLocusNames=ERGA_CDS_06990;
OS   Ehrlichia ruminantium (strain Gardel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=302409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gardel;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000255|HAMAP-Rule:MF_00328}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00328};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00328}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00328}.
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DR   EMBL; CR925677; CAI28151.1; -; Genomic_DNA.
DR   RefSeq; WP_011155353.1; NC_006831.1.
DR   AlphaFoldDB; Q5FFZ9; -.
DR   SMR; Q5FFZ9; -.
DR   EnsemblBacteria; CAI28151; CAI28151; ERGA_CDS_06990.
DR   GeneID; 56785440; -.
DR   KEGG; erg:ERGA_CDS_06990; -.
DR   HOGENOM; CLU_001715_1_0_5; -.
DR   OMA; EWAVVHG; -.
DR   OrthoDB; 1502854at2; -.
DR   BioCyc; ERUM302409:ERGA_RS03585-MON; -.
DR   Proteomes; UP000000533; 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   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03263; guanyl_kin; 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..209
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000266321"
FT   DOMAIN          9..188
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         16..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
SQ   SEQUENCE   209 AA;  24376 MW;  31C2FBBFAD2B49B6 CRC64;
     MNNNLKSRGI MLVMSSPSGG GKTTISQLLV NELQGEIIRS VSVTTREPRN EEVEGKDYFF
     VTEDEFHHLC NTNQMLEYAK VFGNYYGIPR RFVMDNINNG ISILFSIDWQ GAFKLIDIMS
     EHVVSVFILP PSMEELKRRL YNRSGESDMI NQRLKEAAFE ISHCYRYNYI IVNHNIEESV
     QQIKSIFIAE KLKTHRKMFL EQVVKSYYI