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
//