ID A0A1W2CGX5_9FLAO Unreviewed; 734 AA.
AC A0A1W2CGX5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SMC84316.1};
GN ORFNames=SAMN05660703_2971 {ECO:0000313|EMBL:SMC84316.1};
OS Cellulophaga tyrosinoxydans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=504486 {ECO:0000313|EMBL:SMC84316.1, ECO:0000313|Proteomes:UP000192360};
RN [1] {ECO:0000313|EMBL:SMC84316.1, ECO:0000313|Proteomes:UP000192360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21164 {ECO:0000313|EMBL:SMC84316.1,
RC ECO:0000313|Proteomes:UP000192360};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC is a mediator of the stringent response that coordinates a variety of
CC cellular activities in response to changes in nutritional abundance.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; FWXO01000006; SMC84316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2CGX5; -.
DR STRING; 504486.SAMN05660703_2971; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000192360; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
DR InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR NCBIfam; TIGR00691; spoT_relA; 1.
DR PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF19296; RelA_AH_RIS; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:SMC84316.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192360};
KW Transferase {ECO:0000313|EMBL:SMC84316.1}.
FT DOMAIN 402..463
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 734 AA; 84029 MW; D83436B40FE9269F CRC64;
MTEAAIEKEN KQIAKQYKEL LRISYQTLTE DDKKLIRSAF DVAVDAHKNQ RRKSGEAYIF
HPIAVAKIVA SEIGLDAVSI ASALLHDVVE DTEYTLDDIE RMFGEAVARI VDGLTKIAHL
KKDMNISQQA ENFRKMLLTL NDDIRVIIIK IADRYHNMLT MDSMPEYKQV KIASETLYIY
APLAHRIGLY NIKTELEDLS LKYTEPEVYN DILGKIEETK EEQKEYIENF SAVIGDSLDK
ENLNYHIKGR MKSIYSIRRK MVTQNVTFDE IYDKFAIRII YKSDKQNEKF LAWKIYSIVT
DHFTPNPVRL RDWISSPKST GYEALHITVM GPMGKWVEVQ IRSERMHEIA EKGYAAHFKY
KHGNQKEQGI EEWLNKLQEA LENANTNAVD FVEEFKLNLY SKEIFVFTPK GELKSLPKNS
TPLDFAFNIH TEVGMHTRGA KVNGKLVPLN TTLNSGDQVE IITSENAQPN QSWLDYATTA
RARAKIKSTL REEKKSVALE GKEILRRKLR SQKVNFSEDT INKMVLYFKL KTSLDLFYRV
GIGAIDNQKI KDFTSSDNNA FINFFKNKIR RAQTVEDIDK DEITSKYDLL VFGKEEEKLP
YKLSPCCNPI PGDDVFGFVS INEGIKVHSK NCPNAIALQS NYAYRIMSAK WIDSSQQEFT
SEINLTGIDN LGLVSKITEV ISGNMHVNMR NLNFSTDGGT FKGHITVVVK NNEILKKLIN
NLKGINGIDK VTRI
//
