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Database: UniProt
Entry: A0A2V4AIE1_9PSEU
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ID   A0A2V4AIE1_9PSEU        Unreviewed;       789 AA.
AC   A0A2V4AIE1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:PXY19695.1};
GN   ORFNames=BAY60_31060 {ECO:0000313|EMBL:PXY19695.1};
OS   Prauserella muralis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Prauserella.
OX   NCBI_TaxID=588067 {ECO:0000313|EMBL:PXY19695.1, ECO:0000313|Proteomes:UP000249915};
RN   [1] {ECO:0000313|EMBL:PXY19695.1, ECO:0000313|Proteomes:UP000249915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45305 {ECO:0000313|EMBL:PXY19695.1,
RC   ECO:0000313|Proteomes:UP000249915};
RA   Ruckert C., Albersmeier A., Jiang C.-L., Jiang Y., Kalinowski J.,
RA   Schneider O., Winkler A., Zotchev S.B.;
RT   "Draft genome sequence of Prauserella muralis DSM 45305, isolated from a
RT   mould-covered wall in an indoor environment.";
RL   Submitted (JUL-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}.
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:PXY19695.1}.
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DR   EMBL; MASW01000007; PXY19695.1; -; Genomic_DNA.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000249915; 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:PXY19695.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249915};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PXY19695.1}.
SQ   SEQUENCE   789 AA;  87584 MW;  DD0E17FE00F163F0 CRC64;
     MSQELDSVVA AQSDGDARAS QSSTQQERTA GHGGATRAPS ATRRVRARLA RRITAQRAAS
     VKQVLEPLAA IHRELHPNAD LTLLQRAYDV AEELHRDQRR KSGDPYITHP LAVATILAEL
     GMDTTTLVAA LLHDTVEDTG YSLEQLATDF GDKVAQLVDG VTKLDKVKLG TAAEAETIRK
     MVIAMARDPR VLVIKLADRL HNMRTMRFLP PEKQARKAKE TLEVLAPLAH RLGMATVKWE
     LEDLAFAILQ PKKYDEIVRL VADRAPSRDT YLRWVIGELT KQLEQSRLTA KVEGRPKHYY
     SIHQKMIVRG RDLDDIHDLV GVRILVEDVR DCYAAMGVVH ALWQPMPGRF KDYIAQPRFG
     VYQSLHTTVI GPDGKPLEVQ IRTHEMHRTA EYGIAAHWRY KESRGTHGNN PANAVDVDEM
     AWMRQLLDWQ REAADPGEFL ESLRYDLATR EIFVFTPKGD VITLPVGSTP VDFAYAVHTE
     VGHRCIGARV NGRLVALERK LENGEVVEIF TSKAEGAGPS RDWLSFAGSP KARAKIRQWF
     AKERRDEAVE AGKEAITKEV RKVGLPIQRL VSADSMGAVA KELRHPDISS LYAAVGEGHT
     SAKHVVQRLV ALIGGVEEAE EELAERATPS TVTRRRGVGD VGVIVKGESD IWAKLARCCT
     PVPGDEILGF VTRGGGVSVH RTDCTNADDL RTQPERLVEV EWAPSESSVF LVAIQVEALD
     RHRLLSDVTK VLADERVNIL SASVTTSRDR VAVSRFTFEM GDPKHLGHVL KVVRNVEGVY
     DVYRVTSAS
//
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