ID B8CJP3_SHEPW Unreviewed; 735 AA.
AC B8CJP3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
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 OrderedLocusNames=swp_1353 {ECO:0000313|EMBL:ACJ28140.1};
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849 {ECO:0000313|EMBL:ACJ28140.1, ECO:0000313|Proteomes:UP000000753};
RN [1] {ECO:0000313|EMBL:ACJ28140.1, ECO:0000313|Proteomes:UP000000753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877 {ECO:0000313|Proteomes:UP000000753};
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ28140.1; -; Genomic_DNA.
DR RefSeq; WP_020911518.1; NC_011566.1.
DR AlphaFoldDB; B8CJP3; -.
DR STRING; 225849.swp_1353; -.
DR KEGG; swp:swp_1353; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000000753; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000313|EMBL:ACJ28140.1}.
FT DOMAIN 402..463
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 662..735
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 735 AA; 83486 MW; C47025690A84A6D7 CRC64;
MVSVREAHFS DPDFQLEEWV KRYISDSNEA NTLLELIEQV ELLVGQDKKT KTPVLERARE
MIEILAPLNM DIETLQAAIL FVVFDADLIS EEEIQERFGA KLEILVSSVQ TMNAIGALKV
DNQTRNGEPQ IDNIRKMLLA MVEDVRAVVI KLAERICLLR EIKNADEEVK VLIAREIADV
YAPLANRLGI GQLKWELEDI SFRYLHPQTY KDIAKQLDGK RIDRETFIDD FVSQLQARLD
KDQIRAKVYG RPKHIYSIWK KMNGKQLKFD ELFDVRAVRI VTDRLQDCYG ALGVVHTLWH
HIPREFDDYV ANPKPNGYQS IHTIVVGPEG KTVEIQIRTE QMHEDAELGV AAHWKYKEGS
ASGKQSGYEE KINWLRKILQ WQEDVAESGN LVDEVRSQVF EDRVYVFTPS GEVVDLPLGS
TVLDFAYYIH SHVGHKCIGA KVDGRIVQFT YQVETGQRIE IITSKNPNPK RDWLNPNLGY
IKTSRARSKI QHWFKQQDRD KNIVAGREML ETELARTNLK IKDAQSAVER FNMVSMDDLL
AGIGGGDVRL NQVVNHVQSK LRTNELSDEE VLEDLVKKSQ SKPARKGKGQ VEVDGVGNLM
SHIAKCCQPV PGDEIFGFIT KGRGISVHRA DCDQVKELIR AHPERSVEVV WGENYSGGYK
IRIRVFASDR SGLLRDLTFV LAAEKSNVLS MSSSSDVKTQ TATIELELEL YNLDGLSRVI
AKLSQVDGVS EARRV
//
