ID   KGUA_STAEP              Reviewed;         130 AA.
AC   P0C0M8; Q8CSW4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   13-SEP-2023, entry version 62.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8;
DE   AltName: Full=GMP kinase;
DE   Flags: Fragment;
GN   Name=gmk;
OS   Staphylococcus epidermidis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MCL13231, MCL8040, MCL8192, MCL8544, and MCL8827;
RA   Anderson A.S., Wang X.-M., McClements W., Noble L., Jansen K.;
RT   "Establishment of a multilocus sequence typing system for Staphylococcus
RT   epidermidis.";
RL   Submitted (OCT-2002) 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}.
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DR   EMBL; AY163289; AAO60568.1; -; Genomic_DNA.
DR   EMBL; AY163290; AAO60569.1; -; Genomic_DNA.
DR   EMBL; AY163291; AAO60570.1; -; Genomic_DNA.
DR   EMBL; AY163292; AAO60571.1; -; Genomic_DNA.
DR   EMBL; AY163293; AAO60572.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C0M8; -.
DR   SMR; P0C0M8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004385; F:guanylate kinase activity; IEA:UniProtKB-EC.
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   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; Transferase.
FT   CHAIN           <1..130
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170609"
FT   DOMAIN          1..130
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT   VARIANT         109
FT                   /note="K -> R (in strain: MCL8544)"
FT   NON_TER         1
SQ   SEQUENCE   130 AA;  15153 MW;  196E9DB081333C00 CRC64;
     KIFEDPTTSY KYSISMTTRH MREGEIDGVD YFFKTKEEFE ALIKDDQFIE YAQYVGNYYG
     TPVQYVKDTM EEGHDVFLEI EVEGAKQVRK KFPDALFIFL APPSLDDLKE RLVGRGTESD
     EKIQSRVNEA
//