ID A0A3G9IYE3_9ACTN Unreviewed; 762 AA.
AC A0A3G9IYE3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:BBH16328.1};
GN Name=relA {ECO:0000313|EMBL:BBH16328.1};
GN ORFNames=Back2_06150 {ECO:0000313|EMBL:BBH16328.1};
OS Nocardioides baekrokdamisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1804624 {ECO:0000313|EMBL:BBH16328.1, ECO:0000313|Proteomes:UP000271573};
RN [1] {ECO:0000313|EMBL:BBH16328.1, ECO:0000313|Proteomes:UP000271573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 39748 {ECO:0000313|EMBL:BBH16328.1,
RC ECO:0000313|Proteomes:UP000271573};
RA Kang S.W., Lee K.C., Kim K.K., Kim J.S., Kim D.S., Ko S.H., Yang S.H.,
RA Shin Y.K., Lee J.S.;
RT "Complete genome sequence of Nocardioides baekrokdamisoli strain KCTC
RT 39748.";
RL Submitted (NOV-2018) 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}.
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DR EMBL; AP019307; BBH16328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9IYE3; -.
DR KEGG; nbe:Back2_06150; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000271573; Chromosome.
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:BBH16328.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000271573};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BBH16328.1}.
FT DOMAIN 85..182
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 425..488
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 688..762
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 84768 MW; FFD72F67BB348644 CRC64;
MEDAERSPAP PRERGVIARD ASSARSMRTR LARVGRTSGG NPVLEPLFRA VRTNHPKADL
ALLERAYLTA ERFHEGQLRK SGDPYITHPL AVTVILAELG MTEATLVAAL LHDTVEDTPY
TLEELTVDFG GEVAALVDGV TKLDKVHYGE NAQAETIRKM VVAMSKDIRV LVIKLADRLH
NMRTLRYVPQ KSQERSARET LDIYAPLAHR LGMNTIKWEL EDLAFATLHP KIYDEIVRLV
ADRAPSRDQF LADVIKQVEG DLTDAKIKAT VTGRPKHYYS IYQKMVVGGK EFTDIYDLVG
IRILVDNDRD CYSVLGVLHS RWSPVLGRFK DYVAIPKFNL YQSLHTTVIG PAGKAVEMQI
RTFSMHRRAE YGVAAHWKYK ENGRNAVDTE RRSDADMGWV KQLMDWQSEV QDPGEFLDSL
RFEMNRSEVY VFTPKGDVIA LPADATPVDF AYAVHTEVGH RTVGARVNGR LVPLESSLKS
GDSVEVLTSR APTAGPSQDW LMFVKSQRAR SKIRQWFTKE RREEAIEKGQ EQIAKLIRKD
GHSLKRLMSH ESLSTVAAHF NLADVSALYA AVGEGNIGAQ AVVHRVEHEH GLEDQEVVRA
EPVHRPRRSP VLGGDAGVVV AGSPEIWVKL AKCCTPVPPD EILGFVTKGG GVSVHRTDCT
NAAELKAQPE RLVDVEWAPT GNSSFLVNIQ VEALDRARLL SDITMAISDA HVNILSASLT
TSRDRVAKSK FTFEMADAKH LNTVLNAVRH VPGVFDAYRI TA
//
