ID A0A1N6MTV6_9GAMM Unreviewed; 745 AA.
AC A0A1N6MTV6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
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 Name=relA {ECO:0000313|EMBL:SIP72293.1};
GN ORFNames=XIS1_1410032 {ECO:0000313|EMBL:SIP72293.1};
OS Xenorhabdus innexi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=290109 {ECO:0000313|EMBL:SIP72293.1, ECO:0000313|Proteomes:UP000196435};
RN [1] {ECO:0000313|Proteomes:UP000196435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB1681 (deposited as PTA-6826 in the American Type Culture
RC Collection) {ECO:0000313|Proteomes:UP000196435};
RA Gaudriault S.;
RL Submitted (DEC-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. {ECO:0000256|ARBA:ARBA00025704}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; FTLG01000048; SIP72293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6MTV6; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000196435; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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:SF31; 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:SIP72293.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196435};
KW Transferase {ECO:0000313|EMBL:SIP72293.1}.
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; 84651 MW; 8F00B7C7549A6B4B CRC64;
MVAVRSAHLT PAGEFAVDKW IASLNIVNPQ SSQKLVETWR YCHEKVQDHP NAELLLWRGV
EMVEILSTLS MDNDSMRAAL LFPLLDARLL NSETVTEAFG QPIMDLVHGV LEMDAIRELK
ATHTDATCSV QVDNVRRMLL AMVEDFRCVI IKLAERIAYL REVKDASEDE RVLVAKECSN
IYAPLANRLG IGQLKWELED FCFRYLHPDE YKKIARLLHE RRIDREQYIE KFITTLRRYM
LKEGISGEIY GRPKHIYSIW RKMQKKSLAF DELFDVRAVR IVVDRLQDCY AALGIVHTHY
RHLPDEFDDY VANPKPNGYQ SIHTVVLGPN GKTLEIQIRT RQMHDDAELG VAAHWKYKEG
TAIGGGKSGS YESRIAWLRK LIAWQEEMAD TGEMLDEVRS QVFDDRVYVF TPKGDVIDLP
AGSTPLDFAY HIHSDVGHRC IGAKIGGRIV PFSYQLQMGD QIEVITQKQP NPSRDWLNPN
LGYVTTSRGR AKIHNWFRKQ DRDKNIIAGR QMLDSELAHL GVTIKEAEKE LIVRYNVNSL
EEVLAGIGVG DIRIHQLTNF LQSKFNKTTA EEADREALRT LENKTFAPRN SKKDNGRVVV
EGVGNLMHHI ARCCQPIPGD EITGFITRGR GISIHRADCD QLTELEASAP ERVVDAVWGE
SYSSGYSLVV RLLANDRSGL LRDITTILAN EKVNVLGVSS RSDVKQQLAT IDMNIEIYNL
QVLGRVLAKL NQLPDVIEAR RLHGN
//