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Database: UniProt
Entry: D5C0B5_NITHN
LinkDB: D5C0B5_NITHN
Original site: D5C0B5_NITHN 
ID   D5C0B5_NITHN            Unreviewed;       712 AA.
AC   D5C0B5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
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   OrderedLocusNames=Nhal_1289 {ECO:0000313|EMBL:ADE14441.1};
OS   Nitrosococcus halophilus (strain Nc4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE14441.1, ECO:0000313|Proteomes:UP000001844};
RN   [1] {ECO:0000313|Proteomes:UP000001844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG   US DOE Joint Genome Institute;
RA   Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA   Klotz M.G.;
RT   "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT   aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL   Submitted (APR-2010) 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; CP001798; ADE14441.1; -; Genomic_DNA.
DR   RefSeq; WP_013032332.1; NC_013960.1.
DR   AlphaFoldDB; D5C0B5; -.
DR   STRING; 472759.Nhal_1289; -.
DR   KEGG; nhl:Nhal_1289; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000001844; Chromosome.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000001844};
KW   Transferase {ECO:0000313|EMBL:ADE14441.1}.
FT   DOMAIN          381..442
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          635..710
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          539..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  79800 MW;  FE10659321D4C7F6 CRC64;
     MVSTQHNFKH LPLPSASELE EARALLTSQA PEKQVASLLA QGNAVAELLA ELGVDTETQS
     AGLLLPAMEM GVLNPAVITK ELGPAITRLL RGAERLAVLK HYRSSEKDPT QAEKLRKMLL
     AIVEDPRVVL VRLADHLYRL RHAKNALEAT RQTLGQETLD IFAPLANRLG IWQLKWELED
     LALRYLEPET YQQLARALDE RRIDRERYIA KIKAQLKDAL TQAGLRGEVS GRPKHLYSIW
     KKMRNKNLDF HQLFDVHAFR VIVDDVSACY ATLSLVHTLW TPIPEEFDDY IANPKPNGYR
     SLHTAVLGPG KKPMEIQIRS FQMHGESELG VASHWRYKEG AALDTAFEQR IAWLRSFLDR
     KEGSSDNTDL IEQFKSKAFH DRIYVLTPQG RVIDLPEGST PLDFAYAIHT EVGHRCRGAK
     VDGAMVALTQ PLASGQKVEI LTTREGTPSR DWLNPRLGYL HTASARTKIQ RWFKQRDHDL
     HVARGRTLLE RERQRVKLAE VDLAPLLKRF RHPRPDSLLA ALGRGDISLG QLNTALREQR
     PEAPPPTPEQ SARPAPSATA ENAVHVLGVS NLLSRLARCC SPIPGDPIIG YITQGGGVAI
     HRRDCPNITK LSPERRDRLV DVAWHSQQGE THSMDISIQA EDRKGLLHDI TSLLAQKDVN
     ILTINTLSDR SSGQAHMRLT IEVSDTGQLN GLLKRLTRIP GVMEARRSDP GK
//
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