ID A0A0R2JPH8_9LACO Unreviewed; 205 AA.
AC A0A0R2JPH8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Guanylate kinase {ECO:0000256|ARBA:ARBA00016296, ECO:0000256|HAMAP-Rule:MF_00328};
DE EC=2.7.4.8 {ECO:0000256|ARBA:ARBA00012961, ECO:0000256|HAMAP-Rule:MF_00328};
DE AltName: Full=GMP kinase {ECO:0000256|ARBA:ARBA00030128, ECO:0000256|HAMAP-Rule:MF_00328};
GN Name=gmk {ECO:0000256|HAMAP-Rule:MF_00328};
GN ORFNames=IV52_GL000456 {ECO:0000313|EMBL:KRN79051.1};
OS Fructilactobacillus lindneri DSM 20690 = JCM 11027.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1122148 {ECO:0000313|EMBL:KRN79051.1, ECO:0000313|Proteomes:UP000051565};
RN [1] {ECO:0000313|EMBL:KRN79051.1, ECO:0000313|Proteomes:UP000051565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20690 {ECO:0000313|EMBL:KRN79051.1,
RC ECO:0000313|Proteomes:UP000051565};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC {ECO:0000256|ARBA:ARBA00003531, ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000283, ECO:0000256|HAMAP-
CC Rule:MF_00328};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family.
CC {ECO:0000256|ARBA:ARBA00005790, ECO:0000256|HAMAP-Rule:MF_00328}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRN79051.1}.
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DR EMBL; JQBT01000032; KRN79051.1; -; Genomic_DNA.
DR RefSeq; WP_056997624.1; NZ_MIYK01000001.1.
DR AlphaFoldDB; A0A0R2JPH8; -.
DR STRING; 53444.AYR59_05725; -.
DR GeneID; 61250336; -.
DR PATRIC; fig|1122148.6.peg.475; -.
DR OrthoDB; 9808150at2; -.
DR Proteomes; UP000051565; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00328}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00328};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00328};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00328}; Reference proteome {ECO:0000313|Proteomes:UP000051565};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00328}.
FT DOMAIN 5..184
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00328"
SQ SEQUENCE 205 AA; 23295 MW; EB1E4A5085AE57E5 CRC64;
MAKRGMLIVL SGPSGVGKGT VRKALFEDPT VDFNYSISMT TRQPRDGEKN GVDYFFVTKE
EFEDHIKNGE MLEYAKYVDN YYGTPLKYVN DQLNAGHDVF LEIEVNGALQ VRANCPDGVF
IFLTPPDIKE LRNRLVGRGT DNIDIINKRI QKASKEIRMM QNYDYAVVND TINNAVSQIK
DIVKSERLKV KRVMPDYLTS LGDDI
//
