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Database: UniProt
Entry: A0A1Q2GZC3_9GAMM
LinkDB: A0A1Q2GZC3_9GAMM
Original site: A0A1Q2GZC3_9GAMM 
ID   A0A1Q2GZC3_9GAMM        Unreviewed;       718 AA.
AC   A0A1Q2GZC3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=B0W48_12155 {ECO:0000313|EMBL:AQQ00484.1};
OS   Pseudoalteromonas aliena.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=247523 {ECO:0000313|EMBL:AQQ00484.1, ECO:0000313|Proteomes:UP000188243};
RN   [1] {ECO:0000313|EMBL:AQQ00484.1, ECO:0000313|Proteomes:UP000188243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EH1 {ECO:0000313|EMBL:AQQ00484.1,
RC   ECO:0000313|Proteomes:UP000188243};
RA   Kim E., Heo E., Kim H., Kim D.;
RT   "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT   strain EH1 isolated from Arctic seawater.";
RL   Submitted (FEB-2017) 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; CP019628; AQQ00484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2GZC3; -.
DR   STRING; 247523.B0W48_12155; -.
DR   KEGG; paln:B0W48_12155; -.
DR   Proteomes; UP000188243; Chromosome.
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; 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   Kinase {ECO:0000313|EMBL:AQQ00484.1};
KW   Transferase {ECO:0000313|EMBL:AQQ00484.1}.
FT   DOMAIN          393..454
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          644..718
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   718 AA;  80658 MW;  6136896EE633A50D CRC64;
     MVATRQSHQQ DETGDFATRL KELGLSAEKA ELLNQAQALC VNCNNEKQQN TAIEMVEILA
     ELNLDAESLA TAYLTPYFLN DVVLLDTVEE LLGNNVAILL TGVAQMATIS TLSHQGKGSV
     QVDNIRKMLL TMVEDVRAVV IKLAEQVCHL RNVKDADEED RVIAAKETAD IFAPLANRLG
     IGQLKWELED LSFRYLRPDI YKSIAKQLDD KRLAREAYME DMVEQVKSRL SEAGIEAEVY
     GRPKHIYSIY KKMAQKNYEF DQLFDIRAMR IVVERLQDCY GALGIVHTNW RHLNKEFDDY
     VATPKQNGYQ SIHTVVFGPE GKTVEIQIRT SDMHQDAELG VAAHWIYKEG ALPGRGSGYE
     QKISWLRKLL QWQEEVVDGG DLAEELKNQV VEDRVYIFTP SGDIIDLPLG ATPLDFAYYI
     HSNVGHRCIG AKVFGKIVPF THQLTTGDQV EILTQKQPNP SRDWLNPSLG YIKSSRARAK
     IHHWFKQLDR DKNLSAGKDI LDNELQKLGL NYKDLAPAIK RFNFKELDDL MVAIGAGDVR
     LNQMLNFVTD RTEDEPVIRF KNPTKVSGDK NGIVVDGVGS LMSHVAKCCR PVPGDAIIGY
     ITQGRGIGVH KDDCDSFNNL KEQHPERVLS VSWSDDINGS YALSIKIEAT DRSGLIRDIS
     SVLANEKVNV LNMNVNTVTD NQLAIFTMQI EVHDLSGTNR VLSKLHQIEG VHDAKRGH
//
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