ID   KGUA_RICPR              Reviewed;         197 AA.
AC   Q9ZCH7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
GN   Name=gmk; OrderedLocusNames=RP765;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235273; CAA15193.1; -; Genomic_DNA.
DR   PIR; A71637; A71637.
DR   RefSeq; NP_221117.1; NC_000963.1.
DR   RefSeq; WP_004599646.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCH7; -.
DR   SMR; Q9ZCH7; -.
DR   STRING; 272947.RP765; -.
DR   EnsemblBacteria; CAA15193; CAA15193; CAA15193.
DR   GeneID; 57569888; -.
DR   KEGG; rpr:RP765; -.
DR   PATRIC; fig|272947.5.peg.801; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_0_5; -.
DR   OMA; EWAVVHG; -.
DR   Proteomes; UP000002480; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..197
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170596"
FT   DOMAIN          7..185
FT                   /note="Guanylate kinase-like"
FT   BINDING         14..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   197 AA;  23009 MW;  73C4C8430F726B48 CRC64;
     MKFKNKGLII ILSSPSGTGK SSLAKELLKI DNNLRLSISV TTRKPRLGEV DGINYYFKSD
     REFKTLVKQN KFLEYAKIYN DYYGTPKEYV KMLLKQGFDV LFDIDWQGVR SIKKNTNNVI
     TIFILPPSIE ILEQRLRNRA TDNEETIKLR MQSAQNEISH ANEYDYVVIN DDFSQTLKKI
     HEIIVAERAK NFAYHEY