ID A0A495ANA6_9ENTR Unreviewed; 742 AA.
AC A0A495ANA6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=D8M09_00880 {ECO:0000313|EMBL:RKQ41536.1};
OS Enterobacter sp. R1(2018).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=2447891 {ECO:0000313|EMBL:RKQ41536.1, ECO:0000313|Proteomes:UP000271976};
RN [1] {ECO:0000313|EMBL:RKQ41536.1, ECO:0000313|Proteomes:UP000271976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1(2018) {ECO:0000313|Proteomes:UP000271976};
RA Ontanon O.M., Ghio S., Rivarola M., Campos E.;
RT "Enterobacter sp. from a bacterial cellulose degrading consortium draft
RT genome.";
RL Submitted (OCT-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKQ41536.1}.
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DR EMBL; RCAA01000006; RKQ41536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495ANA6; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000271976; 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: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:RKQ41536.1};
KW Transferase {ECO:0000313|EMBL:RKQ41536.1}.
FT DOMAIN 55..160
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 667..742
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 742 AA; 84325 MW; E6BC92AB7BB9B1A4 CRC64;
MVAVRSAHLN KAGEFAPDKW IESLGIASQQ SCERLAETWR YCEQQTKGHP DAELLLWRGV
EMVEILSMLS MDNDTLRAAL LFPLADADVV SEEVMRESID SQVVTLIHGV RDMAAIRQLK
AAHTDSVSAE QVDNVRRMLL AMVDDFRCVV IKLAERIAHL REVKDAPEDE RVLAAKECTN
IYAPLANRLG IGQLKWEMED YCFRYLHPAE YKRIAKLLHE RRIDREHYID EFVASLRKSM
KEEGVKAEVY GRPKHIYSIW RKMQKKSLAF DELFDVRAVR IVAERLQDCY AALGIVHTHF
RHLPDEFDDY VANPKPNGYQ SIHTVVLGPH GKTIEIQIRT KQMHEESELG VAAHWKYKEG
NARSGNTGHE DRIAWLRKLI AWQEEMADSG EMLDEVRSQV FDDRVYVFTP KGDVVDLPAG
STPLDFAYHI HSDVGHRCIG AKIGGRIVPF TYQLQMGDQI EIITQKQPNP SRDWLNPNLG
YVTTSRGRAK IHNWFRKQDR DKNILAGRQI LDDEIERLGI SLKEAEKHLL PRYNFNEIDE
LLAAIGGGDI RLNQMSNFLQ AQFNKPTAAE QDEQALRQLK QKTYAPQSRS KDNGRVVVEG
VGNLMHHIAR CCQPIPGDEI VGFITQGRGI SIHRADCDQL AELQFQAPER IVDAVWGESY
SSGYSLVVRV TANDRSGLLR DITTILANEK VNVLGVASRS DTKQQLATID MNIEIYNLQV
LGRVLGKLNQ VPDIIDAKRL HG
//
