ID A0A1Y4C6U9_9BACT Unreviewed; 742 AA.
AC A0A1Y4C6U9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=GTP pyrophosphokinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B5F81_06510 {ECO:0000313|EMBL:OUO42694.1};
OS Muribaculum sp. An287.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC Muribaculum.
OX NCBI_TaxID=1965623 {ECO:0000313|EMBL:OUO42694.1, ECO:0000313|Proteomes:UP000243574};
RN [1] {ECO:0000313|Proteomes:UP000243574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An287 {ECO:0000313|Proteomes:UP000243574};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO42694.1}.
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DR EMBL; NFIX01000007; OUO42694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4C6U9; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000243574; Unassembled WGS sequence.
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; 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; 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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000243574}.
FT DOMAIN 58..162
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 415..478
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 742 AA; 85033 MW; 6B4F5364DB14A48D CRC64;
MTEFTKEDIG MVQAAYEDLL EAAKKRVQGP NELEMIKKAF EFANEAHKGV RRRSGEPYIM
HPLAVAKIVV SEIGLGYKSI VAALLHDVVE DTDYTIDDIK AQFNEKIASL VDGLTKIKVA
LNNEDTATKT SLQAENFKRI LYTLNDDIRV VLIKLADRLH NIRTIGAMPE YKRDKILGET
MYIFIPLAHR LGLYGIKSEM EDTWLRYKEP EAYRDITEKL ADIQQGNFHK LDKFVAPIEE
ALKEAGISYT ILKRLKSPYS IWYKIKTKGV SFDQIYDLFA VRIIYRPDKP EKEISECFEI
YTILKKIFPP RSFKQDRYRD WVGNPKSNGY EALHCTIMCR DEAKGFWVEV QIRSERMNDI
AEKGIAAHWL YKKDGVILPD MENEMDTMLQ RVREIINNPD ASSIELLDEF HKEMTSPNIT
VFTPKGEQRT LIKGATALDY AYQIHTQIGN TAIAAKINQK LYPLSQELRS GDQVEIITAD
NAAPKAEWLE FLKTAKAINI VKSYLKGEKQ EYIDAGMKTV EQKLHECGLK FSEKNIKLLY
RGYKLNTAED LYFNVGSGML SLSDIEYVLK RMSSNQSWFS WFRNPFKNDN IFVDEASKGM
NFVISPCCNP IPGDPIIGFK DTDNVIHIHK KSCKKATELE SKQGYTIVKD PVWNTENRNH
SYPARISVYG MDRLGILSDV TKYISFVMGV NIRHLDFNSN GGVFTGDIDL LVTSKKDLDT
IIKKLTKIDG IEKVRREDIV EI
//
