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}.
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; 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
//