ID A0A1T2KS55_9GAMM Unreviewed; 741 AA.
AC A0A1T2KS55;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:OOZ35631.1};
GN ORFNames=BOW51_11080 {ECO:0000313|EMBL:OOZ35631.1};
OS Solemya velesiana gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1918948 {ECO:0000313|EMBL:OOZ35631.1, ECO:0000313|Proteomes:UP000190896};
RN [1] {ECO:0000313|EMBL:OOZ35631.1, ECO:0000313|Proteomes:UP000190896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Se-Cadez {ECO:0000313|EMBL:OOZ35631.1};
RA Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT "Mixed transmission modes and dynamic genome evolution in an obligate
RT animal-bacterial symbiosis.";
RL Submitted (NOV-2016) 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:OOZ35631.1}.
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DR EMBL; MPRJ01000088; OOZ35631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T2KS55; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000190896; 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; 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; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:OOZ35631.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190896};
KW Transferase {ECO:0000313|EMBL:OOZ35631.1}.
FT DOMAIN 405..468
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 667..741
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 741 AA; 84690 MW; A58463FB1F0377DF CRC64;
MVSITTKLPA GDSLDERDIR AWLESLSDTW SAEELKYLQR ACDLAVEVHK EEREESGETK
LRHALSVAEI LADMDLDWET LVAAILHDVL PGDRVDSEML EQEFSPAVVR MVEDMARIGG
LTNAQVSDRH QSETEHKENL RRMLLSIADD IRVVLIVLAE RLHEMRILKN FPEAVCAREA
KESQEIYAPL ANRLGIWQIK WELEDLCLRY LEPDSYKELA GMLDGRRAER EVFIRSVIDL
LGKKFADIGI NAQVYGRPKH IYSIWKKMKR KSVPFEQIFD LRAVRVLVDS VAECYGALGV
VHGLWRHIPG EFDDYIATPK VNMYRSIHTA VIGPEDKPLE IQIRTHDMHN HAELGVAAHW
RYKESGGKED PAFQKRIVLM RNWLELKDEP SESDDFVENI KTEFEAQQVY VLTPQGKVME
LPKGATAVDF AYAIHSAVGH RCRGARINGR IAPLTQPLES GQTVEVITVK EGGPSRDWLS
PHHGYLKTSK ARNRVRHWFK QQDYEEHLRL GRSSLDREII RLGVNKPDLN KAAQRFNMKR
GDDLLAAIGR GEVSPVQVAG MGERQFPAVE PEQVEEVAKR KRVTKKKHRK GQGEVIVEGV
DDLMTHMARC CKPVPNDEVI GFITRGRGVT VHRRDCKVVR NLDEANKERL VQVVWAEQPS
DTTYPVDIRV FANDRKGLLR DISSILTNEE VDVLGVNTQS DRKQDRATMR FTIEITDMRQ
LSRILEKVSQ LPDVLDVRRQ V
//
