ID   A0A1G6N6W1_9GAMM        Unreviewed;       772 AA.
AC   A0A1G6N6W1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=SAMN05421749_1092 {ECO:0000313|EMBL:SDC63174.1};
OS   Acinetobacter marinus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=281375 {ECO:0000313|EMBL:SDC63174.1, ECO:0000313|Proteomes:UP000242317};
RN   [1] {ECO:0000313|Proteomes:UP000242317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3699 {ECO:0000313|Proteomes:UP000242317};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-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}.
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DR   EMBL; FMYK01000009; SDC63174.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6N6W1; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000242317; 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; 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; 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:SDC63174.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242317};
KW   Transferase {ECO:0000313|EMBL:SDC63174.1}.
FT   DOMAIN          434..497
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          696..770
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   772 AA;  88731 MW;  3EBB8A4ADB3A0B31 CRC64;
     MVTVREELPS RLNESVAVTT GEHAAETQID LMAWLARIEQ LNGSHQLDLL SQAGHAALEL
     ELSSAVRHRT NSFAMGVGMA DILAHLHVDE HTLVAAMLYR SVREGFIDLQ TLERDFGRDV
     LQLVQGALAM GKLSDLIEQN EHLEDHFNNN KREHLTGIYK MLISVTEDVR VVLIKLAERT
     YSLRQLNQAS KERQERVARE VLTIYAPLAH RLGIAQLKWE LEDLAFRYLS PDRYKEIASL
     LNEKRTEREH YIQHVIDSLK HELAENDIQA EITGRAKHIY SIYRKMRSKN LSFDQLYDIR
     ALRVLVNNVP ECYHALGIVH QMWRHIPHQF DDYITNPKAN GYRSLHTAVI AENKSLEIQI
     RTQDMHQEAE LGVCSHFNYK EGEKRTDQSF NHRLHSLRSV LENYQERKEA QPENLVDEDE
     QDQENLEALQ DFEGFEKIYV FSRDGDIKEL PRDSTVLDFA YHVHTEVGNR CYAARVNQRY
     VPLTYVLKTG EQVEILTKKD REPNRDWLVN SLGYIKTARA RDKLRHWFRQ QDRTKNIEVG
     RETLHKELTR LAIHPKSIDL NDYSQYFNVK SGDDILVALV TGDIGLHSLM NQVNKQMHLD
     ADEPELVLKP TLNPRASHTL SAHGILIDGL DNVELHIARC CQPVHGESIG GYITLNRGVS
     IHKIACSDYL RMIENEPERG VEADWEMQPT RGQSVQIMVE AYDRRGLLKD LTQVIFADHV
     NIRQVNTLSD SDGIANLKLL IEVKGLAQLS KLLARLEQQP GIISARRLVQ GS
//