ID A0A1K1S8J0_9PSEU Unreviewed; 784 AA.
AC A0A1K1S8J0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SFW80325.1};
GN ORFNames=SAMN04489730_4949 {ECO:0000313|EMBL:SFW80325.1};
OS Amycolatopsis australiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW80325.1, ECO:0000313|Proteomes:UP000182740};
RN [1] {ECO:0000313|EMBL:SFW80325.1, ECO:0000313|Proteomes:UP000182740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW80325.1,
RC ECO:0000313|Proteomes:UP000182740};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FPJG01000006; SFW80325.1; -; Genomic_DNA.
DR RefSeq; WP_072478488.1; NZ_FPJG01000006.1.
DR AlphaFoldDB; A0A1K1S8J0; -.
DR STRING; 546364.SAMN04489730_4949; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000182740; 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:SFW80325.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFW80325.1}.
FT DOMAIN 104..201
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 445..506
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 708..782
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 86464 MW; E32EDA7295140FAE CRC64;
MSQELDAAVP AKQGAQQNGQ AAAQPAPPKP NGAAPSPSAT RRVRARLARR ITAQRAAPVK
QVLEPLAVIH RELHPNADLG LLQRAYDVAE ELHRNQRRKS GDPYITHPLA VATILAELGM
DTTTLVAALL HDTVEDTGYA VESLKADFGE KVAELVDGVT KLDKVKLGTS AEAETIRKMV
IAMAKDPRVL VIKLADRLHN MRTMRFLPPE KQARKARETL EVLAPLAHRL GMATVKWELE
DLAFAILQPK KYDEIVRLVA DRAPSRDIYL RSVITDLTSN LVSSRITAKV EGRPKHYYSI
HQKMIVRGRD LDDIHDLVGV RILVEDVRDC YAAMGVVHAL WQPVPGRFKD YIAQPRFGVY
QSLHTTVIGP DGKPLEVQIR TYEMHRTAEY GIAAHWRYKE TKGTHTGNAM DVDEMAWMRQ
LLDWQREAAD PGDFLESLRY ELAAREIFVF TPKGDVITLP VDSTPVDFAY AVHTEVGHRC
IGARVNGRLV ALERKLENGE VVEIFTSKAE NAGPSRDWLQ FAGSPKARAK IRQWFAKERR
DEAIEGGKEA ITKEIRKVGL PIQRLVSAES MGAVATELRH ADISSLYAAV GEGHTSAKHV
VQRLVALIGG VDAAEEELAE RATPSTVTRR RGSNDVGVVV KGASDVWAKL ARCCTPVPGD
EILGFVTRGG GVSVHRTDCT NAGDLKSQPE RLVEVEWAPS ASSVFLVAIQ VEALDRHRLL
SDVTKVLADE KVNILSASVT TSRDRVAVSR FSFEMGDPKH LGHVLKVVRG VEGVYDVYRV
TSAS
//
