ID M4U5K3_9GAMM Unreviewed; 737 AA.
AC M4U5K3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 Name=relA {ECO:0000313|EMBL:AGH80397.1};
GN ORFNames=PCNPT3_02275 {ECO:0000313|EMBL:AGH80397.1};
OS Psychromonas sp. CNPT3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=314282 {ECO:0000313|EMBL:AGH80397.1, ECO:0000313|Proteomes:UP000010320};
RN [1] {ECO:0000313|EMBL:AGH80397.1, ECO:0000313|Proteomes:UP000010320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNPT3 {ECO:0000313|EMBL:AGH80397.1,
RC ECO:0000313|Proteomes:UP000010320};
RA Lauro F.M., Chastain R.A., Stratton T.K., Ferriera S., Johnson J.,
RA Yayanos A.A., Bartlett D.H.;
RT "The complete genome sequence of the deep-sea bacterium Psychromonas
RT CNPT2.";
RL Submitted (MAR-2013) 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; CP004404; AGH80397.1; -; Genomic_DNA.
DR RefSeq; WP_015464278.1; NC_020802.1.
DR AlphaFoldDB; M4U5K3; -.
DR STRING; 314282.PCNPT3_02275; -.
DR KEGG; psy:PCNPT3_02275; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000010320; Chromosome.
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:AGH80397.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010320};
KW Transferase {ECO:0000313|EMBL:AGH80397.1}.
FT DOMAIN 53..158
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 402..463
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 664..737
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 737 AA; 84003 MW; F091B04FC3770B05 CRC64;
MVSVRDTHFY QTAQKNPQKW VTTFNLSLQD QHSLLENYEK VISLCTDPKQ YPLLELGTEM
VEILVTLNMD MDTLNAALVF PLLDNQILSP EKVHELWHKR IAKLVCGAAE MEGFRALQYQ
GLNKISASQV DNLRHMLLAM VEDVRAVVIK LAERICYLRQ VKNASEETKV LLAREVTSIY
APLANRLGIG QLKWELEDLA FRYLQPTIYK KIAKQLAEKR MHRENYVQDF VGRVQELLGE
VHVQGVAYGR PKHIYSIYLK MQKKNLKFEE LFDVRAIRVV VEKLQDCYAA LGAIHTQWHH
IPSEFDDYIA NPKANGYQSI HTVVLGAQGQ SVEVQIRTQK MHDDAELGVA AHWKYKEGTA
GGKSASGYEE KIAWLRKLLA WQEDIAEDDS LVEEVRSQVF DDRVYVFTPQ GEVIDLPAGA
TPLDFAYYIH SQIGHRCIGA KISNHIVPFT YQLKTGDQVE ILTQKEENPS RDWLNLSLGY
IKAPRTRHKI ATWFRKQDRD KNVQAGREVL EVELSKMKLK LTDVTPAIAR FNVNCADDIF
AGIGNGDLRI NQLLHFLNNH HHQQTLEEQD LAVLEALEKR RHIPTPKVSG NNIIIDGVGN
LMHSIARCCQ PVPGDDIEGY ITQGRGISVH RKHCVQLDDL REAHPERIIE ATWGNKQSSG
YALTIRLEAL DRNGLVKDIT TFLSNEKVKM LSMNSTSNFK LRIAVIDLNI EVQNNGDINK
LINQLNLLQD VTGVRRL
//
