ID A0A1C4DT13_9ENTR Unreviewed; 745 AA.
AC A0A1C4DT13;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=GA0061070_101844 {ECO:0000313|EMBL:SCC34544.1};
OS Kosakonia oryziphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kosakonia.
OX NCBI_TaxID=1005667 {ECO:0000313|EMBL:SCC34544.1, ECO:0000313|Proteomes:UP000198515};
RN [1] {ECO:0000313|Proteomes:UP000198515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=REICA_142 {ECO:0000313|Proteomes:UP000198515};
RA Varghese N., Submissions Spin;
RL Submitted (AUG-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; FMBC01000018; SCC34544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4DT13; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000198515; 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; 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: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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:SCC34544.1};
KW Transferase {ECO:0000313|EMBL:SCC34544.1}.
FT DOMAIN 55..160
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 405..466
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 669..744
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 745 AA; 84193 MW; E700C86A85A74D78 CRC64;
MVAVRSAHLN KAGEFDPAKW IASLGITNQL SCERLTETWE YCLRQTQGHP DAGVLLWRGI
EMVEILSMLS MDIDTLRAAL LFPLADAEVV SEDVLRESVG ASVVNLIHGV RDMAAIRQLK
ATHTDSVSSE QVDNVRRMLL AMVDDFRCVV IKLAERIAHL REVKDAPEDE RVLAAKECTN
IYAPLANRLG IGQLKWELED YCFRYLHPAE YKRIAKLLHE RRIDREHYID EFVGHLRAEM
KTEGVKAEVY GRPKHIYSIW RKMQKKHLAF DELFDVRAVR IVAERLQDCY AALGIVHTHY
RHLPDEFDDY VANPKPNGYQ SIHTVVLGPG GKTVEIQIRT RQMHEDAELG VAAHWKYKEG
TAVAGSPRSA HEDRIAWLRK LIAWQEEMAD SGELLDEVRS QVFDDRVYVF TPKGDVVDLP
AGSTPLDFAY HIHSDVGHRC IGAKIGGRIV PFTYQLQMGD QIEIITQKQP NPSRDWLNPN
LGYVTTSRGR SKIHAWFRKQ DRDKNILAGR QILDDELAHL GISLKEAEKH LLPRYNFNEL
EELLAAIGGG DIRLNQMVNF LQSQFNKPSA EEQDAAALKQ LQQKTYTPQN RSKDNGRVVV
EGVGNLMHHI ARCCQPIPGD EIVGFITQGR GISIHRADCD QLEELRTVAP ERIVDAVWGE
SYSAGYSLVV RVTANDRSGL LRDITTILAN EKVNVLGVAS RSDTKEQLAT IDMNIEIYNL
QVLGRVLGKL NQVPDVIDAR RLHGG
//
