ID   KGUA_LISMO              Reviewed;         205 AA.
AC   Q8Y672;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 119.
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}; OrderedLocusNames=lmo1827;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591981; CAC99905.1; -; Genomic_DNA.
DR   PIR; AC1303; AC1303.
DR   RefSeq; NP_465352.1; NC_003210.1.
DR   RefSeq; WP_003725659.1; NZ_CP023861.1.
DR   PDB; 3TAU; X-ray; 2.05 A; A/B=1-205.
DR   PDBsum; 3TAU; -.
DR   AlphaFoldDB; Q8Y672; -.
DR   SMR; Q8Y672; -.
DR   STRING; 169963.gene:17594512; -.
DR   PaxDb; 169963-lmo1827; -.
DR   EnsemblBacteria; CAC99905; CAC99905; CAC99905.
DR   GeneID; 985464; -.
DR   KEGG; lmo:lmo1827; -.
DR   PATRIC; fig|169963.11.peg.1872; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_2_9; -.
DR   OrthoDB; 9808150at2; -.
DR   PhylomeDB; Q8Y672; -.
DR   BioCyc; LMON169963:LMO1827-MONOMER; -.
DR   Proteomes; UP000000817; 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   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   Reference proteome; Transferase.
FT   CHAIN           1..205
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170558"
FT   DOMAIN          5..184
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   STRAND          7..11
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   HELIX           18..27
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   TURN            50..52
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   HELIX           59..67
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   STRAND          71..77
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   STRAND          99..102
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   HELIX           105..114
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   STRAND          118..124
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   TURN            126..130
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   HELIX           144..159
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   STRAND          163..168
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   HELIX           172..187
FT                   /evidence="ECO:0007829|PDB:3TAU"
FT   HELIX           190..200
FT                   /evidence="ECO:0007829|PDB:3TAU"
SQ   SEQUENCE   205 AA;  23282 MW;  40579D7F0038C9E1 CRC64;
     MTERGLLIVL SGPSGVGKGT VREAVFKDPE TSFDYSISMT TRLPREGEQD GVDYYFRSRE
     VFEQAIKDGK MLEYAEYVGN YYGTPLEYVE EKLAAGVDIF LEIEVQGAMQ VRKAMPEGIF
     IFLTPPDLSE LKNRIIGRGT ESMEVVEERM ETAKKEIEMM ASYDYAVVND VVANAVQKIK
     GIVETEHLKT ERVIHRYKKM LEGLQ
//