ID B0T3H1_CAUSK Unreviewed; 705 AA.
AC B0T3H1;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=Caul_1728 {ECO:0000313|EMBL:ABZ70857.1};
OS Caulobacter sp. (strain K31).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ70857.1};
RN [1] {ECO:0000313|EMBL:ABZ70857.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31 {ECO:0000313|EMBL:ABZ70857.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) 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; CP000927; ABZ70857.1; -; Genomic_DNA.
DR AlphaFoldDB; B0T3H1; -.
DR STRING; 366602.Caul_1728; -.
DR KEGG; cak:Caul_1728; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_5; -.
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 Transferase {ECO:0000313|EMBL:ABZ70857.1}.
FT DOMAIN 23..122
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 371..432
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 631..705
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 705 AA; 78650 MW; 46A155228B25AAB0 CRC64;
MNRAYVYAMR MHGSQTRASG DPYYAHPIEV AGILTEYRLD TATIVTALLH DVIEDTPVTK
EEIGKLFGEE IAELVEGVTK LSKLELQTEH SRQAENLRKF ILAISKDVRV LLVKLADRLH
NMRTLHFIKS QAKRERIARE TRDIYAPLAR NIGCHRICTE LEELSFEHTN PVARTAIIRR
LDTLRAEQGG AVALVSQEIA ARLESAGLPA RVFGREKSPY SIWRKLQRKS IGFSQMSDIY
AFRVIVDSED DCYRALGVVH RAWSSVPERF KDFISTPKRN NYRSLHTTVV GPRGMRIEMQ
IRTEAMDRVN EEGVAAHFRY KDASYGLDLE GMEAAGGRDP LANLRQLVQV LEHGGDAEEL
VEHAKLEMFL DQVFVFTPKG KLVSLPRGAM PLDFAYAVHT SVGDTCIGVK INGELKPLRT
LLNNGDVVEV VRGSKPVVPP DWRSLTVTGR ARSAIRRHIR QTEKEEFLRL GRASVEQVFE
RAGKKLKDVS LRPILERYAL DTEEALFDAV GRGRVSPSQV LETAFPGMKD TDVAVATARR
KIEGGTAARL YVRGGGLTPG VSLHFAHCCS PVPGDRIVGI LREDGANGQD GGLDVHTIDC
PKLAEYEDRE DLWRDLNWTP EAERETVSLA RLHATIGNAP GVLGQVCTII GEAGGNIVNL
RMHHRQSDFF DVDIDVEVRD AKHLTNISAA LRTCPTVETV DRTRG
//
