ID V6JX21_STRRC Unreviewed; 855 AA.
AC V6JX21;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:EST21434.1};
GN ORFNames=M878_37120 {ECO:0000313|EMBL:EST21434.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST21434.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST21434.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST21434.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
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:EST21434.1}.
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DR EMBL; AWQX01000324; EST21434.1; -; Genomic_DNA.
DR RefSeq; WP_023552079.1; NZ_CM002285.1.
DR AlphaFoldDB; V6JX21; -.
DR STRING; 1352936.M878_37120; -.
DR PATRIC; fig|1352936.5.peg.7700; -.
DR HOGENOM; CLU_012300_3_0_11; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000017984; 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:EST21434.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000017984};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EST21434.1}.
FT DOMAIN 159..256
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 511..572
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 776..850
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 95043 MW; 66226CF0A1DC2BE3 CRC64;
MPDEAQPLTA AKPEPASAPA AKPAPHASNA KNDTRGPIEH AQSAPVEKAA EATRPKPSPA
LDPARAGGPP APERPVQPPV VRQPAGQART GSSNRVRARL ARLGVQRANP YNPVLEPLLR
IVRSNDPKIE NSTLRQIERA YQVAERWHRG QKRKSGDPYI THPLAVTTIL AELGMDPATL
MAGLLHDTVE DTEYGLDQLR RDFGDTVALL VDGVTKLDKV KFGEAAQAET VRKMVVAMAK
DPRVLVIKLA DRLHNMRTMR YLKREKQEKK ARETLEIYAP LAHRLGMNTI KWELEDLAFA
ILYPKMYDEI VRLVAERAPK RDEYLAIVTD EVQADLRAAR IKATVTGRPK HYYSVYQKMI
VRGRDFAEIY DLVGIRVLVD TVRDCYAALG TVHARWNPVP GRFKDYIAMP KFNMYQSLHT
TVIGPNGKPV ELQIRTFDMH RRAEYGIAAH WKYKQEAVAG ASKVRTDVPK AGKDKDAIND
MAWLRQLLDW QKETEDPGEF LESLRFDLSR NEVFVFTPKG DVIALPAGAT PVDFAYAVHT
EVGHRTIGAR VNGRLVPLES TLDNGDLVEV FTSKAPGAGP SRDWLGFVKS PRARNKIRAW
FSKERRDEAI EQGKDAIVRA MRKQNLPIQR ILTGDSLVTL AHEMRYSDIS ALYAAIGEGH
VSAQNIVQKL VQALGGEEAA TEEIDETVPP SRSRSRKRRS SADPGVVVKG VEDVWVKLAR
CCTPVPGDPI IGFVTRGSGV SVHRSDCVNV DSLSREPERI LDVEWAPTQS SVFLVAIQVE
ALDRSRLLSD VTRVLSDQHV NILSAAVQTS RDRVATSRFT FEMGDPKHLG HVLKAVRGVE
GVYDVYRVTS GRSRS
//
