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Database: UniProt
Entry: A0A1N6MTV6_9GAMM
LinkDB: A0A1N6MTV6_9GAMM
Original site: A0A1N6MTV6_9GAMM 
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
//
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