KGUA_STAES
ID KGUA_STAES Reviewed; 207 AA.
AC P0C0M9; Q8CSW4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SE_0885;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-154.
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: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; AE015929; AAO04482.1; -; Genomic_DNA.
DR EMBL; AY163288; AAO60567.1; -; Genomic_DNA.
DR RefSeq; NP_764440.1; NC_004461.1.
DR RefSeq; WP_001830096.1; NZ_WBME01000001.1.
DR AlphaFoldDB; P0C0M9; -.
DR SMR; P0C0M9; -.
DR STRING; 176280.SE_0885; -.
DR EnsemblBacteria; AAO04482; AAO04482; SE_0885.
DR GeneID; 50018977; -.
DR KEGG; sep:SE_0885; -.
DR PATRIC; fig|176280.10.peg.858; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_2_9; -.
DR OMA; EWAVVHG; -.
DR Proteomes; UP000001411; 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..207
FT /note="Guanylate kinase"
FT /id="PRO_0000170610"
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"
SQ SEQUENCE 207 AA; 24065 MW; 4C70F7F4BCFB8EDE CRC64;
MDKEKGLLIV LSGPSGVGKG TVRKKIFEDP TTSYKYSISM TTRHMREGEI DGVDYFFKTK
EEFEALIKDD QFIEYAQYVG NYYGTPVQYV KDTMEEGHDV FLEIEVEGAK QVRKKFPDAL
FIFLAPPSLD DLKERLVGRG TESDEKIQSR VNEARKEVEM MNLYDYVVVN DEVELAKNRI
QSIVEAEHLK RERIEAKYRK MLLEVKK