ID A0A147EQT6_9MICO Unreviewed; 748 AA.
AC A0A147EQT6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:KTR86855.1};
GN ORFNames=NS354_02570 {ECO:0000313|EMBL:KTR86855.1};
OS Leucobacter chromiiresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR86855.1, ECO:0000313|Proteomes:UP000070810};
RN [1] {ECO:0000313|EMBL:KTR86855.1, ECO:0000313|Proteomes:UP000070810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS354 {ECO:0000313|EMBL:KTR86855.1,
RC ECO:0000313|Proteomes:UP000070810};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
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:KTR86855.1}.
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DR EMBL; LDRK01000013; KTR86855.1; -; Genomic_DNA.
DR RefSeq; WP_058593054.1; NZ_LDRK01000013.1.
DR AlphaFoldDB; A0A147EQT6; -.
DR PATRIC; fig|1079994.3.peg.444; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000070810; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd00077; HDc; 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; IPR003607; HD/PDEase_dom.
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; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 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; SM00471; HDc; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KTR86855.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000070810};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KTR86855.1}.
FT DOMAIN 72..169
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 410..471
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 674..748
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 748 AA; 82788 MW; 76EE83B6383434D6 CRC64;
MASQDTTTGG TTALRRLVPR IFSRGSAPGA VDQLIRTVRG NHPRADLTVI ERAYAVAERA
HRGQKRRSGE PYITHPIAVA QILADLGIAP GVIAAALLHD TVEDTEYTLD QLTQEFGEEI
AMLVDGVTKL DKVKYGDSAQ AETVRKMVVA MAKDIRVLVI KLADRLHNAR TWGFVSGDSA
KRKAQETIEI YAPLAHRLGI QSMKTELEDL SFAVLKPKLY AEIQNLVEQR NPQRDELVGR
VIGAIEGDLR ESKIRGEVTG RPKELYSIYQ KMIVRGREFD DIYDLVGIRV LVNSIRDCYA
VLGAVHARWT PIPGRFKDYI ATPKFNLYQS LHTTVIGPDG RAVEIQIRTV EMHQRAEYGV
AAHWKYKQRQ QNQSQASNDM AWLAHISDWQ AETEDPSEFL DALRYEIGAK EVYVFTPKGR
VIGLPDGGTT VDFAYAVHTE VGHRTMGARV NGRLVPLETA LQNGDVVEVF TSKDPNAGPN
QDWLGFVQSK RAQNKIKQWF TKERREEAAE TGKTEITKAL RKQGLPLHRV MNSSALQQIA
LQLRYLDVTA LYAAVGEGHV SAQSVVEKVT ALVFDEQTST EPALATLPII EAPRAPKTTD
SSGVVVAGAS DVLAKLAKCC TPVPGDEILG YVTKGQGVSV HRVDCHNFMT LRAQEDRVVG
VEWAPTSKSV FLVQIQVEAL DRSGLLSDVT RTLSEHHVNI LSASVNTSSS RLAISKFVFE
MANATHLEHV LNAVRRIDGV YDVYRITN
//
