ID E8RSY2_ASTEC Unreviewed; 817 AA.
AC E8RSY2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN OrderedLocusNames=Astex_2966 {ECO:0000313|EMBL:ADU14603.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU14603.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 2 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) 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 -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; CP002396; ADU14603.1; -; Genomic_DNA.
DR AlphaFoldDB; E8RSY2; -.
DR STRING; 573065.Astex_2966; -.
DR KEGG; aex:Astex_2966; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_5; -.
DR Proteomes; UP000001492; Chromosome 2.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000001492};
KW Transferase {ECO:0000313|EMBL:ADU14603.1}.
FT DOMAIN 143..242
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 486..551
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 743..817
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 91000 MW; 273AED049D3A9F9F CRC64;
MYEKSTVLDM ATEGQSVITA RVSSENEPPA VPPGFPEETP PEVPPGEPKE GDIIPPPEAP
PLDPPAETPP IQTPPEMPSM TQMAQAPKPA PTPAPKRRFL RQMELIDRVA AYDPTVDEAL
LNRAYVYAMR MHGAQLRASG DPYFAHPIEV AGILTDYKLD SAAIVTALLH DTIEDTPATR
EEIASLFGEE IAQLVEGVTK LTRLELKSEY TKQSENLRKF ILAISKDVRV LLVKLADRLH
NMRTLQYVPE HKRERISRET LEVYAPLARQ IGCNRFATEL EDLAFTFINP RGRAAILQRL
ADLRDQKGAA VADIARDIQD TLSVAGIEAR VSGREKSPYS IWRKLQRKSI GFSQLSDIVA
FRVIVDSPDD CYLSLGVLHR KWPCVQDRFK DFISTPKSNN YQSLHTTVIG HKGARIEMQI
RTEVMDRVAE EGLAAHWGYK NQAYGFDEAA ATQWAERNPI ANLRAIVQIA ENGGDSDEWV
EHAKLEMFLD QVFCFSPKGR LISLPRGAMP LDFAYAVHTE VGDKAIGAVI NGEHKPLRTP
LQNGDQVEII TGVEARVNPD WQSLTITGRA RAAIRRSIRQ TQRDDFIRLG RSALERGAAQ
VEKTLTDMSW RPAFERFQVQ SEDELFELCG RGKIAPAKVL EALFPGLKLP ATLTTDSFSR
IKDGEDATAF VRGHALRPQQ KIVFSRCCTP VPGDRIVGIV EGAAVHVHSI ECEQLEAYEG
QKEVWIDLQW TLNAEKNTVS PARIRANMRN KPGVLGQVCT LIGEAKGNIV NIRLSNQQVD
FLDAEFEVEV LDARHLTNIT AAIRTNPSVE GVERIRG
//
