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Database: UniProt
Entry: D4XDQ6_9BURK
LinkDB: D4XDQ6_9BURK
Original site: D4XDQ6_9BURK 
ID   D4XDQ6_9BURK            Unreviewed;       621 AA.
AC   D4XDQ6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:EFF75128.1};
DE            EC=3.1.7.2 {ECO:0000313|EMBL:EFF75128.1};
DE   Flags: Fragment;
GN   Name=spoT {ECO:0000313|EMBL:EFF75128.1};
GN   ORFNames=HMPREF0004_3603 {ECO:0000313|EMBL:EFF75128.1};
OS   Achromobacter piechaudii ATCC 43553.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=742159 {ECO:0000313|EMBL:EFF75128.1, ECO:0000313|Proteomes:UP000004510};
RN   [1] {ECO:0000313|Proteomes:UP000004510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43553 {ECO:0000313|Proteomes:UP000004510};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT   "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL   Submitted (MAR-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}.
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:EFF75128.1}.
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DR   EMBL; ADMS01000079; EFF75128.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4XDQ6; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_0_0_4; -.
DR   Proteomes; UP000004510; Unassembled WGS sequence.
DR   GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016779; F:nucleotidyltransferase 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; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
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; 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; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EFF75128.1}.
FT   DOMAIN          97..196
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          438..499
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   NON_TER         621
FT                   /evidence="ECO:0000313|EMBL:EFF75128.1"
SQ   SEQUENCE   621 AA;  68732 MW;  B6A38B5E2C96C165 CRC64;
     MAFPGLKYAS SGLLAALRAG SRLGRRTGKK GKNPATPPSV AAQEAADATA SPVASLAPLT
     EIIGSYLEPK DVERVREAYR FADQAHLGQF RASGSPYISH PIAVTEICAG WKLDVNALSA
     ALLHDVMEDQ GIAKHELAEK FGPEVAELVD GLSKLDRLDF ATKAEQQAES FRKMLLAMAR
     DVRVILIKLA DRLHNMRTLD AVNPEKRRRI ARETLDIYAP IAHRLGLNLL FRELQDLCFA
     AMYPNRYQVL YKAVLAARGN RREVITKIAD SVRASLPAAG IEAEVTGREK TLYGIYRKMV
     DQKKSFSDVL DIYGFRVIVH TLPECYLALG TLHQLYRPVP GKFKDYIAIP KVNGYQSLHT
     TLVGPYGTPV EFQFRTRDMH HVAEEGVASH WLYKGADLTL NDLQKRTHQW LQSLLDIQSQ
     TGDSGEFLEH VKVDLFPDAV YVFTPRGKII SLPRGATPVD FAYAIHTDIG NQAVAAKVNG
     EFVPLRTELN SGDTVEIVTS PASRPNAQWL NYVRTGRARS EIRHYLRTVK YEESVAFGER
     LLSQALQELH MPMPATDDPA WQKLARSTGA SSREEILADI GLGKRLAAVV ARRFAPEHQL
     VATTAAAVDE LTSARSAPIL I
//
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