ID S5SUT1_9CORY Unreviewed; 760 AA.
AC S5SUT1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=GTP pyrophosphokinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B841_07380 {ECO:0000313|EMBL:AGS34949.1};
OS Corynebacterium maris DSM 45190.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS34949.1, ECO:0000313|Proteomes:UP000015388};
RN [1] {ECO:0000313|EMBL:AGS34949.1, ECO:0000313|Proteomes:UP000015388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT 45190).";
RL Submitted (NOV-2012) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
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; CP003924; AGS34949.1; -; Genomic_DNA.
DR RefSeq; WP_020934882.1; NC_021915.1.
DR AlphaFoldDB; S5SUT1; -.
DR STRING; 1224163.B841_07380; -.
DR KEGG; cmd:B841_07380; -.
DR PATRIC; fig|1224163.3.peg.1482; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000015388; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd00077; HDc; 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; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
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:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 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; SM00471; HDc; 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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000015388};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 77..174
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 414..479
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 686..760
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 760 AA; 84538 MW; 5AD995E959CFD17C CRC64;
MAQDKIQRRS SPGVRSMSAR LARSLTGSRV RTNPVLDPVL SIHRQFHPKA DAVTLTRAYE
RAEELHQGVY RKSGDPYITH PLAVAAICAE IGMDTTTLVA ALLHDTVEDT DYSLEQLTEE
FGPEVARLVD GVTKLDKVAL GAAAEAETIR KMIVAMANDP RVLVIKVADR LHNMRTMRFL
PPEKQAKKAR QTLEVIAPLA HRLGMASIKW ELEDLSFAIL YPKKYDEIVR LVADRAPSRD
RALHEIIDQT TAALRENGVS AEVQGRPKHY WSIYQKMIVR GRDFDEIFDL VGTRVLVDSV
KDCYAAIGVV HSIYSPLPGR FKDYISNPRF GVYQSLHTTV MAGSGRPLEV QVRTHEMHYN
AEFGVAAHWR YKETKGSHKG DQNEVEQMSW MRQLLDWQKE AADPNEFLDS LRYDLSSQQI
FAFTPKGDVV NLPADSTPVD FAYSVHTEVG HRCIGAKVNG KLVALESPLK SGDRVEIFTS
KDANAGPSRD WQDFVVSPRA KAKIRQWFAK ERREEHLEAG RDALAAEVQR GGLPMHRLFT
ADSMKQVAKQ LHYPDIDALY TAIGAGHVSA QNVMHRLMAI FGDEDDAVDA LAARTPMSEI
INTRAKVADA GEGILVEGSP DVMAKMAKCC LPVPGDEIFG FVTRGGGVSV HRTDCTNAEK
LRQEPERLIR VEWGGMDSAA GAFAATLQVE ALERQGLLAE LTRVLSEQHL SIVALDSHVS
DDRIAMIKFT ITVSDTKQLG TLMTTLRNTE SVFDIYRVNA
//
