ID A0A120MZU3_HALHR Unreviewed; 734 AA.
AC A0A120MZU3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=HH1059_11410 {ECO:0000313|EMBL:BAU57833.1};
OS Halorhodospira halochloris (Ectothiorhodospira halochloris).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=1052 {ECO:0000313|EMBL:BAU57833.1, ECO:0000313|Proteomes:UP000218890};
RN [1] {ECO:0000313|Proteomes:UP000218890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-1059 {ECO:0000313|Proteomes:UP000218890};
RA Tsukatani Y.;
RT "Halorhodospira halochloris DSM-1059 complete genome sequence.";
RL Submitted (FEB-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP017372; BAU57833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A120MZU3; -.
DR KEGG; hhk:HH1059_11410; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000218890; Chromosome.
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; 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; 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; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:BAU57833.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218890};
KW Transferase {ECO:0000313|EMBL:BAU57833.1}.
FT DOMAIN 405..466
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT REGION 565..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 82727 MW; 1D6096E7517F4EF3 CRC64;
MVQTAFTDID DLSTLTVDGW LRRLPARFDS EELGLIAQAW DLARHKGDNL QRQSGESYFE
HGVATATALA GLGLDATTLA AALVHDLPDL DGSYKQILQR KLNADIADLV QGVCRMHGLG
SFHDSAELES AHGSRVEGLR KMLLAMARDV RVVFITLAER LHDLRSAKEM DPSQRQQLAR
ETQEIYAPLA NRLGIWQLKW ELEDLSFRYL EPDSYQELAS MLAERRSDRE VYIQRVRAEL
QAALDEQGVS AQVYGRPKHI FSIYRKMQRK GLRFDELYDL RALRVLVDSV QQCYAAMGIV
HGLWTPIPRE FDDYIATPKE NNYRSLHTAV VGPEGKALEV QIRTHQMHQE AELGIAAHWR
YKEGGKQDAN FERKVAWLRQ LLEWGGEDGE AEDFVDQVRA EVFADRVYAL TPSGDVIDLP
RGATPLDFAY HIHTSLGHRC RGAKINNRIV QLTRQLENGD RVEIMTAREE RPSRDWLNPQ
LGFLYTNRAR SKVRTWFKQR DHDKNVAAGR QVLDKELTRL GVDDVSIEEL ANQSRYQKAE
AFLSALGRGE VTSGHIASLL RNRLLPQRPE PPPANAQARR ATGSEGDITV EGVGNLLTRM
ARCCAPAPGD PIVGFITRGS GVTIHRQDCK DFGHLREREP ERVLDVSWST EPEGRYPVRI
NVRSAELNAV LAEITRLVSS EGARLGGVTT HTEQADSYRT ELDLQVSDVQ QLARLMEKLS
GLENVDSVWR GSSS
//
