ID Q6LMS8_PHOPR Unreviewed; 743 AA.
AC Q6LMS8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 117.
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=Y0811 {ECO:0000313|EMBL:CAG21398.1};
GN OrderedLocusNames=PBPRA3082 {ECO:0000313|EMBL:CAG21398.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG21398.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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}.
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DR EMBL; CR378673; CAG21398.1; -; Genomic_DNA.
DR RefSeq; WP_011219657.1; NC_006370.1.
DR AlphaFoldDB; Q6LMS8; -.
DR STRING; 298386.PBPRA3082; -.
DR KEGG; ppr:PBPRA3082; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_6; -.
DR Proteomes; UP000000593; Chromosome 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000000593}.
FT DOMAIN 54..159
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 669..743
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 681..740
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 743 AA; 84645 MW; 9DCA7AD8B9965D3F CRC64;
MVAVRGAHLK ENDTFELSSW VDSLQQDAKA SKRLKKTYQR CIEITTKEES TPLLLWRGRE
MVEILVTLSM DADTLVAALV VPLVEAGIYQ HEQVKEDYNT TIMQLVKGVE QMAAIGQLNA
TTEGAEQSAQ VDNIRRMLLS MVDDFRCVVI KLAERICNLR EVKDEPDEVR RSAARECANI
YAPLANRLGI GQLKWEIEDY AFRYQHPDVY KQIAKQLSER RIDREYYIDH FVSDLDESMK
ASHIKAEVHG RPKHIYSIWR KMQKKSLEFD ELFDVRAVRI IADQLQDCYA ALGVVHTKYR
HLPKEFDDYV ANPKPNGYQS IHTVVLGPEG KTIEIQIRTK QMHEESELGV AAHWKYKEGS
SSGAAKSSYD EKINWLRKLL VWQEEMSDSG EMLDELRSQV FDDRVYAFTP KGDVVDLPLN
ATPLDFAYHI HSEVGHRCIG AKVEGRIVPF TYHLQMGEQV EIITQKEANP SRDWLNPNLG
FVTSGRARAK VHAWFRRQAH DKNMVAGREI LELELNKIGA KLKDAEVYAL KRFNAKNVDE
LFVGIGSGDL RINQVVNHIS MIINKPTAEE EDQQLVDKLT EASTKISTSA KKPQRDAVVV
EGVDNLMTHL ARCCQPIPGD EIVGFVTQGR GISVHRNDCE QLAELRHHVP ERIIHTVWGG
GFVGNYNITV RVTASERNGL IKELTNTLAN EKAKVAGMKS RIDYKKQMSI MDFDLELTDL
DVLSKVLKRI EQVKDVAEAK RLY
//
