ID   KGUA_SALTY              Reviewed;         207 AA.
AC   Q9X6M5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
GN   Name=gmk; OrderedLocusNames=STM3740;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=LT2;
RX   PubMed=14594851; DOI=10.1128/jb.185.22.6732-6735.2003;
RA   Beck B.J., Huelsmeyer M., Paul S., Downs D.M.;
RT   "A mutation in the essential gene gmk (encoding guanylate kinase) generates
RT   a requirement for adenine at low temperature in Salmonella enterica.";
RL   J. Bacteriol. 185:6732-6735(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC       {ECO:0000269|PubMed:14594851}.
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; AF140283; AAD31506.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22599.1; -; Genomic_DNA.
DR   RefSeq; NP_462640.1; NC_003197.2.
DR   RefSeq; WP_000046969.1; NC_003197.2.
DR   AlphaFoldDB; Q9X6M5; -.
DR   SMR; Q9X6M5; -.
DR   STRING; 99287.STM3740; -.
DR   PaxDb; Q9X6M5; -.
DR   EnsemblBacteria; AAL22599; AAL22599; STM3740.
DR   GeneID; 1255264; -.
DR   KEGG; stm:STM3740; -.
DR   PATRIC; fig|99287.12.peg.3957; -.
DR   HOGENOM; CLU_001715_1_0_6; -.
DR   OMA; EWAVVHG; -.
DR   PhylomeDB; Q9X6M5; -.
DR   BioCyc; SENT99287:STM3740-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
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..207
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170599"
FT   DOMAIN          4..184
FT                   /note="Guanylate kinase-like"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   207 AA;  23499 MW;  A26FF5C1FB40970B CRC64;
     MAQGTLYIVS APSGAGKSSL IQALLKTQPL YDTQVSVSHT TRAPRPGEVH GEHYFFVNHD
     EFKTMIGREA FLEHAEVFGN YYGTSRETIE QVLATGVDVF LDIDWQGAQQ IREKMPQARS
     IFILPPSKIE LDRRLRGRGQ DSEEVIAKRM AQAVAEMSHY AEYDYLIVND DFDTALSDLK
     TIIRAERLRM SRQKQRHNAL ISKLLAD