ID A0A2I1JC42_9MICC Unreviewed; 760 AA.
AC A0A2I1JC42;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Bifunctional (P)ppGpp synthetase/guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:PKY80954.1};
GN ORFNames=CYJ35_00415 {ECO:0000313|EMBL:PKY80954.1};
OS Pseudoglutamicibacter albus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudoglutamicibacter.
OX NCBI_TaxID=98671 {ECO:0000313|EMBL:PKY80954.1, ECO:0000313|Proteomes:UP000234591};
RN [1] {ECO:0000313|EMBL:PKY80954.1, ECO:0000313|Proteomes:UP000234591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0722 {ECO:0000313|EMBL:PKY80954.1,
RC ECO:0000313|Proteomes:UP000234591};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) 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:PKY80954.1}.
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DR EMBL; PKGR01000001; PKY80954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1JC42; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000234591; 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:PKY80954.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 77..174
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 412..475
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 679..753
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 580..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 84659 MW; AAE0FEDD268768C4 CRC64;
MVQQRVGSQP PRRGRSLSRL IRFSGRSSFP AAPPILEPLL RTVRAQNPGE DLTLITRAYD
VAAHWHEGVK RKSGDPYITH PVAVATILAE MGLTGATLAA ALLHDTVEDT EYSLEALRKD
FGDEIALLVD GVTKLDKVTY GEAAQAETVR KMIVAMSQDI RVLMIKLADR MHNARTWRYV
NPESAAKKAR ETLEIYAPLA HRLGMNTVKW ELEDLSFAVL HPKVYEEIVR MVGARTPERE
RYLAQVRQAI EANLTEQKIK AVITGRPKHY YSVYQKMVVR KKDFNEIHDL MGVRILVDSV
KDCYAVLGII HAHWNPLPGR FKDYIAMPKF NMYQSLHTSV IGPGGRPIEV QIRTHEMHQR
AEYGVAAHWK YKQGSQESDQ ETSINWLNRL VAWQKDTQDP DEFLDSLRYV INSAEVYVFT
PAGEVRSLPL GSTPVDFAYA VHTDVGHRAV GAKVNGKLVP LHTPLNNGDQ VEILTSKAEN
AGPSRHWQDF VASPRARTKI RQWFLKERRE EAVEKGQELL SKAIRKAGLP LQKLMTAQIL
NAVAQELHYK DITGLYAGLG EGHVSSKNVM EHITSLTGEP EVAAPEPGLD FTSGQGTSHR
SQPSSSGVIV QGSRDVMAKL APCCSPVPPD SIKGFVTRGS GVTVHRAACP NIANLGGAEA
ERIVDVAWDP RAHTVFTVEI QVEALDRHSL LSDVTKVLSE NHVNILSANL WTTKDRTAIS
RFRFQLGEPD FMSHIFAAIR RIEGVYDVSR VLGGSSEDQQ
//
