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Database: UniProt
Entry: A0A1P8U8T5_9MICO
LinkDB: A0A1P8U8T5_9MICO
Original site: A0A1P8U8T5_9MICO 
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
//
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