ID   KGUA_MYCCT              Reviewed;         297 AA.
AC   Q2SSR8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
GN   Name=gmk; OrderedLocusNames=MCAP_0208;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000123; ABC01818.1; -; Genomic_DNA.
DR   RefSeq; WP_011387096.1; NC_007633.1.
DR   AlphaFoldDB; Q2SSR8; -.
DR   SMR; Q2SSR8; -.
DR   PRIDE; Q2SSR8; -.
DR   EnsemblBacteria; ABC01818; ABC01818; MCAP_0208.
DR   GeneID; 23778839; -.
DR   GeneID; 58110233; -.
DR   KEGG; mcp:MCAP_0208; -.
DR   HOGENOM; CLU_001715_1_0_14; -.
DR   OMA; FLMPPTL; -.
DR   OrthoDB; 770109at2; -.
DR   PhylomeDB; Q2SSR8; -.
DR   Proteomes; UP000001928; 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..297
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000266350"
FT   DOMAIN          4..183
FT                   /note="Guanylate kinase-like"
FT   REGION          204..297
FT                   /note="Unknown"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   297 AA;  34242 MW;  9080733C7E435375 CRC64;
     MKKGKMIIIS GPSGVGKGSV NGELLQNPDL RLKYSVSMTT RKPRNGEING VNYFFVSNEE
     FAKAIVNDEL IEYAHFVGNS YGTPRKYVEQ ELKKGNNVIL EIEVDGATQV LNKEANVLSI
     FLMPPNLTEL ANRIRGRQTE DEEKIKARLD KALLEIPLKH NYQYVIENDN VANAVAKITD
     VLHLEGLTDI KTPTVYERLE QIVEQIVKEK YMYFVNNWET NVKLLAKNEE EKNKAKNFDA
     ETYLIKLLTK KVYHKVLGHG DFSKLLDKDF VDFKIQKLMF KINFFSVEQK HYNNDEF