ID V4NM22_9CAUL Unreviewed; 755 AA.
AC V4NM22;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 ORFNames=AEAC466_15235 {ECO:0000313|EMBL:ESQ82862.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ82862.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ82862.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ82862.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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}.
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:ESQ82862.1}.
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DR EMBL; AWGE01000015; ESQ82862.1; -; Genomic_DNA.
DR AlphaFoldDB; V4NM22; -.
DR STRING; 1282362.AEAC466_15235; -.
DR PATRIC; fig|1282362.3.peg.3012; -.
DR eggNOG; COG0317; Bacteria.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000017826; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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:UP000017826}.
FT DOMAIN 81..180
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 421..489
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 681..755
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 84421 MW; B7E14ED0FB6F4C51 CRC64;
MSSEGEQILE KTSQASEITS AGTVATSASP APNRPKFLRQ IELIDRVAAY DPTVDEAMLN
RAYVYAMKMH GAQLRASGDP YFAHPIEVAG ILTDYKLDAA AIATALLHDT IEDTPATREE
IAEKFGEDVA NMVEGVTKLT RLELQSEYTK QSENLRKFIL AISKDIRVLL VKLADRLHNM
RTLHFVAPEK RERISRETLE VYAPLARSIG CNRFATELED LAFSFINPLA HQAIIHRLEE
MRTEKGATIA AIARDVAAKL EKQGISARVS GREKSPYSIW KKLQRKSVGF AQLSDIYAFR
VVVNNVEECY RALGIMHRAW PCVQERFKDF ISTPKSNNYK SLHTTVVGHK GTRIELQIRT
EEMDRIAEEG VAAHWGYKNQ AYGFDEEAAT RDGGRNPINS LRNIVTIVEN GGDSEDWVEH
AKMEMYLDQV FCFSPKGRLI SLPRGAMPLD FAFAVHTQVG ETAIGCLING EHKPLRTVLQ
NGDQVEILTG LESRVNQDWF SLTVTGRARS AIRRHLRQRE AGDFIKLGRA AIERAAAQVD
KRLEDISWRP AFERFHVANE DALFELCGRG KIFPAKILEA IFPGLKLPLM LTTDTLTRIK
DGVGGAAFVR GSALREHHKV IFSKCCYPVP GDRIVGFVEG DTVHVHSIEC ERLEALESQD
ESWIDLHWTL NAEKNTLSVA RLRVDMQNKP GVLGQACTLI GEAKGNIINI AINAEPMDFL
DVDFDIEVLD ARHITNISAA LRTSPMIESV DRVRG
//
