ID   A0A090K418_9GAMM        Unreviewed;       748 AA.
AC   A0A090K418;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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:CED58463.1};
GN   ORFNames=MVIS_0432 {ECO:0000313|EMBL:CED58463.1};
OS   Moritella viscosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=80854 {ECO:0000313|EMBL:CED58463.1, ECO:0000313|Proteomes:UP000032438};
RN   [1] {ECO:0000313|Proteomes:UP000032438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hjerde E.;
RL   Submitted (SEP-2014) 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}.
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DR   EMBL; LN554852; CED58463.1; -; Genomic_DNA.
DR   RefSeq; WP_045108893.1; NZ_FRDV01000006.1.
DR   AlphaFoldDB; A0A090K418; -.
DR   STRING; 80854.MVIS_0432; -.
DR   KEGG; mvs:MVIS_0432; -.
DR   PATRIC; fig|80854.5.peg.458; -.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   Proteomes; UP000032438; Chromosome complete sequence.
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; 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:CED58463.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032438};
KW   Transferase {ECO:0000313|EMBL:CED58463.1}.
FT   DOMAIN          408..469
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          674..748
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   748 AA;  84834 MW;  087430FC8069DDC1 CRC64;
     MVAVRDSHLT NPEDFDAKTW TSSLALTSTE QDELFELYSQ LALKETADPL MDEAVPDFPL
     LAYGVEMVEI LMTMDMDMDT LKVALLYPFF HAKLYDNEQI ETLFGCKLLP LLIAVVEMDA
     IRTLQAKSQK PSESQVDNLR RMLMAIVDDV RAIVIKLAER ICHLRQVKNE SEEERVLAAK
     EISDIYAPLA NRLGIGQLKW ELEDLSFRYS HPDTYKQIAK LLLERRIDRE EFIDSFVAQV
     KTGVEAAGGK VEVYGRPKHI YSIWKKMQKK NLDFTGLYDV RAVRVIAAEL QDCYAALGVI
     HNLFRPIPSE FDDYVANPKA NGYQSIHTVV AVGDENKAVE VQIRTKQMHD DAELGVAAHW
     RYKEGADTTK KGSYEEKIAW LRKLLAWQDD MTESGSLVDE LRSQVFDDRV YVFTPKGDVV
     DMPQGSTPLD FAYYVHSMVG HRCIGAKISG RIVPFTYELQ TGDQIEIITQ KNPNPSRDWL
     LPNLGYVKSA RARAKINTYF KRLDRDKNVA AGKDMLEGEL HKLKLQLSDA SCAFERFNSN
     TLEDLLAQVG SGDARLNQVI NHIKVLLLQP SAEEEDKLAL ELVDQQVQKS QNQPKKKRNK
     DHIVVEGMGN LMTHIANCCQ PIPGDDIVGY ITQGRGISIH RNGCLQYADL SNRQPERIID
     AVWGDDFSGG YRVTLVVHAT DRRGLLRDLT TIFANDRIHV VGMNTRTDTK LQTATLEINI
     ELYNIDTLSH LTNRMSQVKG VIYAKRLR
//