ID A0A0J1GGW6_9GAMM Unreviewed; 743 AA.
AC A0A0J1GGW6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN Name=relA {ECO:0000313|EMBL:KLU98954.1};
GN ORFNames=ABT58_19805 {ECO:0000313|EMBL:KLU98954.1};
OS Photobacterium aphoticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLU98954.1, ECO:0000313|Proteomes:UP000036426};
RN [1] {ECO:0000313|EMBL:KLU98954.1, ECO:0000313|Proteomes:UP000036426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLU98954.1,
RC ECO:0000313|Proteomes:UP000036426};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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 -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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:KLU98954.1}.
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DR EMBL; LDOV01000040; KLU98954.1; -; Genomic_DNA.
DR RefSeq; WP_047876172.1; NZ_PYMF01000056.1.
DR AlphaFoldDB; A0A0J1GGW6; -.
DR PATRIC; fig|754436.4.peg.4173; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000036426; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 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; 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:SF40; GTP PYROPHOSPHOKINASE; 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; 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; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000036426};
KW Transferase {ECO:0000313|EMBL:KLU98954.1}.
FT DOMAIN 54..159
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 404..465
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 669..743
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 743 AA; 83974 MW; 6D20531A260BC46E CRC64;
MVAVRGAHLK ENETFELSSW INSLKQDGKV ANRLTQTYQR CLDLTEKEAT APLLLWRGRE
MVEILVTLSM DKDTLVAALL FPLVEAGVYA PEQLQEDYGQ TIAQMVAGVS QMAAIGQLNA
TKEGAEQSAQ VDNIRRMLLS MVDDFRCVVI KLAERICNLR EVKDEPDAVR RAAAKECANI
YAPLANRLGI GQLKWEIEDY AFRYRHPDTY KQIAKQLSER RIDREHYIEH FVTDLADSMK
ASNIKAEVQG RPKHIYSIWR KMQKKNLAFD ELFDVRAVRI IADALQDCYA ALGVVHTKYR
HLPKEFDDYV ANPKPNGYQS IHTVVLGPEG KTIEIQIRTK QMHEESELGV AAHWKYKESG
SSSGGAKSSY DEKINWLRKL LAWQEEMSDS GEMLDELRSQ VFDDRVYAFT PKGDVVDLPL
NATPLDFAYH IHSEVGHRCI GAKVEGRIVP FTYHLQMGDQ VEIITQKEPN PSRDWLNPNL
GFVTSSRARA KVHAWFRKQD RDKNIAAGRE ILEHELSKIG ATLKDAEAYA LKRFNVNSAD
ELYAGVGSGD LRINQVLNHI NALVNKPTAE EEDQQLLEKL TEASSKATST KKPQRDAVVV
EGVDNLMTHL ARCCQPIPGD DIQGFVTQGR GISVHRSDCE QLEELRHVAP QRIIDTVWGG
GFVGNYNITV RVTASERNGL LKELTNTLAN EKVKVAGMKS RVDYKKQMSI MDFDLELTDL
DVLGRVLKRI EQVKDVAEAK RLH
//
