KGUA_CAMJE
ID KGUA_CAMJE Reviewed; 207 AA.
AC Q9PNB8; O32356; Q0P979;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase;
GN Name=gmk; OrderedLocusNames=Cj1177;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-126.
RC STRAIN=ATCC 700819 / NCTC 11168;
RA Karlyshev A.V., Wren B.W.;
RL Submitted (SEP-1997) 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; AL111168; CAL35292.1; -; Genomic_DNA.
DR EMBL; AJ000744; CAA04292.1; -; Genomic_DNA.
DR PIR; C81323; C81323.
DR RefSeq; WP_002860253.1; NC_002163.1.
DR RefSeq; YP_002344568.1; NC_002163.1.
DR AlphaFoldDB; Q9PNB8; -.
DR SMR; Q9PNB8; -.
DR IntAct; Q9PNB8; 50.
DR STRING; 192222.Cj1177c; -.
DR PaxDb; Q9PNB8; -.
DR PRIDE; Q9PNB8; -.
DR EnsemblBacteria; CAL35292; CAL35292; Cj1177c.
DR GeneID; 905467; -.
DR KEGG; cje:Cj1177c; -.
DR PATRIC; fig|192222.6.peg.1158; -.
DR eggNOG; COG0194; Bacteria.
DR HOGENOM; CLU_001715_1_2_7; -.
DR OMA; EWAVVHG; -.
DR Proteomes; UP000000799; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..207
FT /note="Guanylate kinase"
FT /id="PRO_0000170515"
FT DOMAIN 5..185
FT /note="Guanylate kinase-like"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 81
FT /note="F -> V (in Ref. 2; CAA04292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 24025 MW; F258896CD6EE1AC2 CRC64;
MKLQGFVLLI SGPSGAGKST LLKKLFDEFE DELYFSISST TRKPREGEKN GIHYHFISHE
EFQKGIDSDH FLEWARVHEN FYGTSLKHTQ NALDNGKIVV FDIDVQGFKI ARKKMADKIV
SVFITTKNKD ELKKRLIKRN TDTIIQLEKR LQNASDEMKE LSEYDYLIIN DELKQSYEAL
RAILIAHKFR TKGQNLGQIQ NIWNEGE