ID   KGUA_STAAC              Reviewed;         207 AA.
AC   Q5HGM3;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
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=SACOL1221;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW38058.1; -; Genomic_DNA.
DR   RefSeq; WP_000368227.1; NC_002951.2.
DR   PDB; 2J41; X-ray; 1.90 A; A/B/C/D=1-207.
DR   PDBsum; 2J41; -.
DR   AlphaFoldDB; Q5HGM3; -.
DR   SMR; Q5HGM3; -.
DR   KEGG; sac:SACOL1221; -.
DR   HOGENOM; CLU_001715_1_2_9; -.
DR   EvolutionaryTrace; Q5HGM3; -.
DR   Proteomes; UP000000530; 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   CDD; cd00071; GMPK; 1.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03263; guanyl_kin; 1.
DR   PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..207
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170603"
FT   DOMAIN          6..185
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   STRAND          8..12
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           19..28
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           60..68
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   STRAND          72..78
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           87..95
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           109..115
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           151..155
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           157..163
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           173..188
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           191..196
FT                   /evidence="ECO:0007829|PDB:2J41"
FT   HELIX           198..204
FT                   /evidence="ECO:0007829|PDB:2J41"
SQ   SEQUENCE   207 AA;  24037 MW;  F17991AA47238DC0 CRC64;
     MDNEKGLLIV LSGPSGVGKG TVRKRIFEDP STSYKYSISM TTRQMREGEV DGVDYFFKTR
     DAFEALIKDD QFIEYAEYVG NYYGTPVQYV KDTMDEGHDV FLEIEVEGAK QVRKKFPDAL
     FIFLAPPSLE HLRERLVGRG TESDEKIQSR INEARKEVEM MNLYDYVVVN DEVELAKNRI
     QCIVEAEHLK RERVEAKYRK MILEAKK
//