ID A2U282_9FLAO Unreviewed; 740 AA.
AC A2U282;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=GTP pyrophosphokinase, RelA/SpoT family {ECO:0000313|EMBL:EAQ41437.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:EAQ41437.1};
GN Name=relA {ECO:0000313|EMBL:EAQ41437.1};
GN ORFNames=MED152_01945 {ECO:0000313|EMBL:EAQ41437.1};
OS Polaribacter sp. MED152.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ41437.1, ECO:0000313|Proteomes:UP000006470};
RN [1] {ECO:0000313|EMBL:EAQ41437.1, ECO:0000313|Proteomes:UP000006470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED152 {ECO:0000313|EMBL:EAQ41437.1};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
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; CP004349; EAQ41437.1; -; Genomic_DNA.
DR RefSeq; WP_015480162.1; NC_020830.1.
DR AlphaFoldDB; A2U282; -.
DR STRING; 313598.MED152_01945; -.
DR KEGG; pom:MED152_01945; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_2_10; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000006470; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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; cd04876; ACT_RelA-SpoT; 1.
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; IPR006674; HD_domain.
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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EAQ41437.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006470};
KW Transferase {ECO:0000313|EMBL:EAQ41437.1}.
FT DOMAIN 59..159
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 740 AA; 84740 MW; 9BEE9C367599A3F5 CRC64;
MEYTATIEEE NKEIANRYKD LLKGTYEVLS KEDKELIRKA FDIAVDAHSK QRRKTGEPYI
FHPIAVAKIV AMEIGLGATS IAAALLHDVV EDTDYTLDDM EQLFGETIAR IVNGLTKISR
LNKEQDASIQ AENFRKMLLT LHDDVRVILI KIADRLHNMQ TMDAMPGYKQ VKIASETLYI
YAPLAHRLGL YNIKTELEDL GLKYTEPDVF NSIVAKIKES KEEQQNYLRR FEDTLKNGLD
KENFTYEIKG RFKSIFSIRR KMQKQNVTFE EVFDKYAIRI IFKPISKDEK HDAWKIYSIV
TDNFRPNPAR LRDWISQPKS TGYEALHITV IGPDAQWVEV QIRSERMNEI AEKGYAAHFK
YKQGDENESG LDVWLNRLKE TLENQSLNAV DFVEDFKLNL YAKEIYVFTP KGDLKSLPKD
ASALDFAFSI HTDIGLKCRG AKVNGKLVPL SYTLRSGDQI EVITSSTNKP NARWLDFVIT
ARAKTKIRAA LKEEEKLIAE EGKAILKRKL RHLKISFNEK TTNELVNFFK LRTSFDLYYR
IGNGAIDNTQ LKAFVSQRNS TILNFFKTKL RRNASPTENA DGTEEITHKY DALVFGKEEE
KLDYKLSKCC NPIPGDQVFG FLTINDGIKV HKKNCPNAIS LQSNYAYRIM QAKWIDSTKQ
DFKVVLHING VDTSGIVNEV TKIISSNMGV FIHSINISGD EGVFDGKISL SVKNSAQLKK
LMNRIQKVEG VKKVERVNRM
//
