ID L7LP27_9ACTN Unreviewed; 764 AA.
AC L7LP27;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=GTP pyrophosphokinase/guanosine-3',5'-bis (Diphosphate) 3-pyrophosphohydrolase {ECO:0000313|EMBL:GAC62890.1};
GN Name=relA {ECO:0000313|EMBL:GAC62890.1};
GN ORFNames=GSI01S_48_00010 {ECO:0000313|EMBL:GAC62890.1};
OS Gordonia sihwensis NBRC 108236.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC62890.1, ECO:0000313|Proteomes:UP000035083};
RN [1] {ECO:0000313|EMBL:GAC62890.1, ECO:0000313|Proteomes:UP000035083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC62890.1,
RC ECO:0000313|Proteomes:UP000035083};
RA Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236.";
RL Submitted (DEC-2012) 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 -!- 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:GAC62890.1}.
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DR EMBL; BANU01000048; GAC62890.1; -; Genomic_DNA.
DR AlphaFoldDB; L7LP27; -.
DR eggNOG; COG0317; Bacteria.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000035083; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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 Hydrolase {ECO:0000313|EMBL:GAC62890.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GAC62890.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000035083};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GAC62890.1}.
FT DOMAIN 81..178
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 425..486
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 688..762
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 764 AA; 84307 MW; 77DF3A3B8A9E0595 CRC64;
MSDPDTKRPD DGSPLSSRRV RARLARRMTA PPRSGVAPVL EPLVSLHREV YPKADVAVLQ
QAYAVAEEAH SGQFRKSGDP YITHPLAVAT ILADLGMDTT TLVAALLHDT VEDTSYSLEK
LEADFGAEVA HLVDGVTKLD KVALGSAAEA ETIRKMIIAM ARDPRVLVIK VADRLHNMRT
MRFLPPEKQA RKARETLEVI APLAHRLGMA TVKWELEDLA FAILHPKKYE EIVRLVADRA
PSRDTYLARV RSDLNTALGA SRITATVEGR PKHYWSIYQK MIVKGKDFDD IHDLVGMRIL
CDEVRDCYAA IGVVHSLWQP MAGRFKDYIA QPSFGVYQSL HTTVIGPEGK PLEVQIRTFE
MHRTAEFGIA AHWRYKEGRK GKGRKATDIA EVDDMAWMRQ LLDWQREAAD PGEFLESLRY
DLAVKEIFVF TPKGDVITLP AGSTPIDFAY AVHTEVGHRC IGARVNGRLV ALERALENGE
VVEVFTSKAE NAGPSKDWQN FVVSPRAKAK IRQWFAKERR EEALEAGKDA IVKEVRRGGL
PVHRLVSGES INALAKEFGF NDVDALYTAV GEGHVPAGRV VHRLVAMLGG VDAAEEEIAN
RATPSSPTRS RQSGDSGVVV EGVDNVLVKL AKCCTPVPGD EILGFVTRGG GVSVHRSDCT
NADDLRSQPE RLVPVSWAPN PSSVFLVAIQ VEALDRHRLL SDVTRVLADE RVNILSASLT
TNRDRVAVSK FTFEMGDPKH LGHVLNVVRN VEGVYDVYRV TSAA
//
