ID   KGUA_BARHE              Reviewed;         222 AA.
AC   Q6G439;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=BH05390;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF27347.1; -; Genomic_DNA.
DR   RefSeq; WP_011180469.1; NZ_LRIJ02000001.1.
DR   PDB; 7LUY; X-ray; 2.30 A; A/B/C/D/E/F=1-222.
DR   PDBsum; 7LUY; -.
DR   AlphaFoldDB; Q6G439; -.
DR   SMR; Q6G439; -.
DR   STRING; 283166.BH05390; -.
DR   PaxDb; Q6G439; -.
DR   PRIDE; Q6G439; -.
DR   EnsemblBacteria; CAF27347; CAF27347; BH05390.
DR   KEGG; bhe:BH05390; -.
DR   eggNOG; COG0194; Bacteria.
DR   OMA; EWAVVHG; -.
DR   Proteomes; UP000000421; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..222
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170500"
FT   DOMAIN          19..197
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00328"
FT   STRAND          21..25
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           32..39
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   TURN            62..64
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   STRAND          65..68
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           71..79
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           98..106
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           117..126
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   STRAND          130..137
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           141..151
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           156..170
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           171..175
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   STRAND          177..181
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           185..200
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           203..205
FT                   /evidence="ECO:0007829|PDB:7LUY"
FT   HELIX           209..218
FT                   /evidence="ECO:0007829|PDB:7LUY"
SQ   SEQUENCE   222 AA;  25925 MW;  7E1DB17DD380479F CRC64;
     MVTFFENELS AKKRNQRRGF LFILSSPSGA GKSTLSRLLL KDGKLELSIS MTTRQKRPSE
     VDGLHYHFIS KKEFKRKRDG NEFIEWAEVH GNYYGTLRES VENVLSTGRD MLFDIDYQGT
     KQLQKKMPGD TVSVFILPPS MKELISRLYR RAEDSQDIIN LRLKNARTEM QHWRSYDYVI
     INENLNQSVS LIKSIYLAET VKRERCFFLE PFINGLIAEK ID