ID A0A1P8U8T5_9MICO Unreviewed; 755 AA.
AC A0A1P8U8T5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Bifunctional (P)ppGpp synthetase/guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:APZ34532.1};
GN ORFNames=BOH66_10000 {ECO:0000313|EMBL:APZ34532.1};
OS Microbacterium aurum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=36805 {ECO:0000313|EMBL:APZ34532.1, ECO:0000313|Proteomes:UP000187185};
RN [1] {ECO:0000313|EMBL:APZ34532.1, ECO:0000313|Proteomes:UP000187185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 15219 {ECO:0000313|EMBL:APZ34532.1,
RC ECO:0000313|Proteomes:UP000187185};
RA Jung Y., Shin J.-H., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "Complete genome sequence of Microbacterium aurum KACC 15219.";
RL Submitted (DEC-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; CP018762; APZ34532.1; -; Genomic_DNA.
DR RefSeq; WP_076690843.1; NZ_JAFBCQ010000001.1.
DR AlphaFoldDB; A0A1P8U8T5; -.
DR STRING; 36805.BOH66_10000; -.
DR KEGG; maur:BOH66_10000; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000187185; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; GTP PYROPHOSPHOKINASE; 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:APZ34532.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000187185};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 76..173
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 418..479
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 680..754
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 83632 MW; 668ED789A05D4821 CRC64;
MTQTPAASAQ NSPQSSSLRR LVPRIFSRAP SRNGVEQLVR TVRTHHPKGD VSIIERAYQV
AAAAHASQKR QSGEPYITHP LAVAQILADL GLGPRAIAAA LLHDTVEDTD YSLDQLAADF
GDEVAMLVDG VTKLDKVKYG DAAQAETVRK MIVAMSKDIR VLLIKLADRL HNARTWGFVP
PEKAAKKATE TLEIYAPLAH RLGIQAVKSE LEDLSFAVLH PKLYAEIDSL VKQRTPQREE
YMHSVIDAVE EDLRDLRIRG RVMGRPKQLY SVYQKMVVRG REFDDIYDLI GIRVLVNNVR
DCYAVLGSIH ARWTPLPGRF KDYIATPKFN LYQSLHTTVI GPGGRTVEIQ IRTNEMHQQA
EYGVAAHWKY KERMAGGKPD AKAVDADMAW LAHISDWQAE TADPGEFLDS LRFEIGAKEV
YVFTPKGRVI GLPAGGTPVD FAYAVHTEVG HRTMGAKVNG RLVPLESELH SGDVVEVFTS
KNPDAGPSQD WLTFVKSTRA RNKIRGWFTK ERREEAVEQG KDAIARAMRR QNLPLQRLMN
QDSFTEVAHQ LRYEDVTALY AAVGEGHIST QSVIEKVTAL VSSQEDTSTG PIEIPHVGRS
KAPRGGDSGV LVRGAPDILV KLAKCCTPVP GDDIVGFVTR GSGVSVHRAD CTNVKSLKDD
PERMIDVAWA PTTKSVFLVH IQVEALDRSG LLSDITRVLS EHHVNILSAS VQTTNDRLAL
SRYVFEMGDI VHLDRVLNAV RRIDAVYDVY RVTSS
//