ID   KGUA_UREPA              Reviewed;         191 AA.
AC   Q9PQS9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
GN   Name=gmk; OrderedLocusNames=UU213;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
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; AF222894; AAF30621.1; -; Genomic_DNA.
DR   RefSeq; WP_006688865.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQS9; -.
DR   SMR; Q9PQS9; -.
DR   STRING; 273119.UU213; -.
DR   EnsemblBacteria; AAF30621; AAF30621; UU213.
DR   GeneID; 29672624; -.
DR   KEGG; uur:UU213; -.
DR   eggNOG; COG0194; Bacteria.
DR   HOGENOM; CLU_001715_1_2_14; -.
DR   OrthoDB; 9808150at2; -.
DR   Proteomes; UP000000423; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..191
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170635"
FT   DOMAIN          4..185
FT                   /note="Guanylate kinase-like"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   191 AA;  22005 MW;  8E552F2E9AF19E9F CRC64;
     MKRGKLIVFS GPSGVGKHTI LSKIINRKDL NLAYSISMTT RKKREGEVNG VDYYFVNDEE
     FKKAILNNEL IEWAEFVGNK YGTPRTIVEK LRDEGKNVIL EIEVVGALKV LDLYKNDDLI
     SIFLLPPSID ELKKRLLKRN TETLETIKKR IQKATHEITI KDYYQYNIIN DNPDHAANQL
     AEIILNEIKQ S
//