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Database: UniProt
Entry: Q1ZNB1_PHOAS
LinkDB: Q1ZNB1_PHOAS
Original site: Q1ZNB1_PHOAS 
ID   Q1ZNB1_PHOAS            Unreviewed;       744 AA.
AC   Q1ZNB1;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
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   ORFNames=VAS14_20411 {ECO:0000313|EMBL:EAS63818.1};
OS   Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS   CCUG 15956)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS63818.1, ECO:0000313|Proteomes:UP000001603};
RN   [1] {ECO:0000313|EMBL:EAS63818.1, ECO:0000313|Proteomes:UP000001603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S14 {ECO:0000313|EMBL:EAS63818.1,
RC   ECO:0000313|Proteomes:UP000001603};
RX   PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA   Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA   DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA   Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA   Robb F.T., Kjelleberg S., Cavicchioli R.;
RT   "The genomic basis of trophic strategy in marine bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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:EAS63818.1}.
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DR   EMBL; AAOJ01000005; EAS63818.1; -; Genomic_DNA.
DR   RefSeq; WP_005371455.1; NZ_CH902602.1.
DR   AlphaFoldDB; Q1ZNB1; -.
DR   SMR; Q1ZNB1; -.
DR   GeneID; 61230661; -.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000001603; 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; 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   Kinase {ECO:0000313|EMBL:EAS63818.1};
KW   Transferase {ECO:0000313|EMBL:EAS63818.1}.
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..744
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   744 AA;  84546 MW;  B7AC772C4D47A40C CRC64;
     MVAVRGAHLK ENTTFELVSW VESLRQDAKV SSRIEGTYQR CIELAAEQEN GPLLLWRGRE
     LVEILVTLSM DADTLIAALL YPLVEGGCYS TDALKEEYSG TILHLVQGVE QMCAISQLKS
     TAEETAQAAQ VDNIRRMLLS MVDDFRCVVI KLAERICNLR EVKDQPDEVR RAAAQECANI
     YAPLANRLGI GQLKWEIEDY AFRYQHPDTY KQIAKQLSER RIDREDYITH FVDDLSDAMK
     ASNIRAEVQG RPKHIYSIWR KMQKKSLEFD ELFDVRAVRI VAEELQDCYA ALGVVHTKYR
     HLPKEFDDYV ANPKPNGYQS IHTVVLGPEG KTIEIQIRTK QMHEESELGV AAHWKYKEGT
     ASGGAQSAYD EKINWLRKLL AWQEEMSDSG EMLDELRSQV FDDRVYAFTP KGDVVDLPSN
     ATPLDFAYHI HSEVGHRCIG AKVEGRIVPF TYHLQMGDQV EIITQKEPNP SRDWLNPNLG
     FVTSSRARAK VHAWFRKQDR DKNIIAGKEI LEAELVKIHA TLKDAQYYAA KRFNVKSPEE
     LYAGIGSGDL RINQVINHIN ALVNKPTAEE EDQQLLEKLS EASNKQATSH KKPQRDAVVV
     EGVDNLMTHL ARCCQPIPGD DIQGFVTQGR GISVHRMDCE QLEELRHHAP ERIIDTVWGG
     GFVGNYTITV RVTASERNGL LKELTNTLMN EKVKVAGMKS RVDYKKQMSI MDFELELTDL
     EVLGRVLKRI EQVKDVAEAK RLYG
//
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