ID A0A2T7FW37_9RHOB Unreviewed; 712 AA.
AC A0A2T7FW37;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DC363_10730 {ECO:0000313|EMBL:PVA06371.1};
OS Thalassorhabdomicrobium marinisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassorhabdomicrobium.
OX NCBI_TaxID=2170577 {ECO:0000313|EMBL:PVA06371.1, ECO:0000313|Proteomes:UP000244817};
RN [1] {ECO:0000313|EMBL:PVA06371.1, ECO:0000313|Proteomes:UP000244817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH-SD16 {ECO:0000313|EMBL:PVA06371.1,
RC ECO:0000313|Proteomes:UP000244817};
RA Ji X.;
RT "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT Bohai Sea.";
RL Submitted (APR-2018) 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}.
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:PVA06371.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QCYG01000006; PVA06371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7FW37; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000244817; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 2.
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 Hydrolase {ECO:0000313|EMBL:PVA06371.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244817}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 382..447
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 627..701
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 712 AA; 80504 MW; 2155989B41C61862 CRC64;
MITADDLITL VRTYNPKTNA KLIADAFAFG AEMHDGQFRH SGEPYFTHPV AVAAILAEQQ
MDDATLITAL LHDTIEDTKA TFSEVEERFG TEIAELVDGV TKLTNLQLHS TETKQAENFR
KLFMATSRDL RVTLVKLADR LHNMRTIRSM RDDKQAQKAR ETMDIYAPLA GRMGMQWMRE
ELEDLAFRVL NPEGRNSIIR RFITLQRETG DVIEKIQTDM ELEMEKAGIA ADIYGRAKKP
YSIWRKMQEK EQGFSRLSDI YGFRVITQTE TDCYLALGAI HQRWRAVPGR FKDYISQPKS
NGYRSLHTTV SGRDGKRVEV QIRTVEMHEV AEAGVAAHWS YRDGIRVENR FAVDPARWIA
QLTERLDEDH DHGEFLDMVK LEMYQDQVFC FTPKGDVIKL PRGATPIDFA YAIHTRIGHA
CVGAKIDGLR VPLWTRIKNG QSVEVITAEG QSPQATWIDI AVTGRAKTAI RRALREEDRE
RFIRLGRELV RVGFENVGKS ATDKALKTAG KFLGLGNVDD LLERVGAAEI TSRDVVTAIY
PELAKSAGNE IESRRAVVGL EANQTHRRAQ CCQPIPGERI VGITYRGEGV VVHAIDCDVL
ATLEDQPERW IDLRWQEGTH SPTNTITLEM TITNDAGVLG RICTLIGEND ANISDLVFID
RKPDYFRLLI EVDLRDTEHM HVIMNVLEAD SNVAAIARHR DPNRAGQVQR QS
//
