ID A0A2T5BIB8_MYCDI Unreviewed; 740 AA.
AC A0A2T5BIB8;
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=C7449_101388 {ECO:0000313|EMBL:PTM98722.1};
OS Mycoplana dimorpha.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Mycoplana.
OX NCBI_TaxID=28320 {ECO:0000313|EMBL:PTM98722.1, ECO:0000313|Proteomes:UP000241247};
RN [1] {ECO:0000313|EMBL:PTM98722.1, ECO:0000313|Proteomes:UP000241247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7138 {ECO:0000313|EMBL:PTM98722.1,
RC ECO:0000313|Proteomes:UP000241247};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
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:PTM98722.1}.
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DR EMBL; PZZZ01000001; PTM98722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5BIB8; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000241247; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:PTM98722.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000241247}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 390..451
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 666..740
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 195..222
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 740 AA; 83133 MW; 400BCDFB8A265997 CRC64;
MMRQYELVER VQQYKPDANE ALLNKAYVYA MQKHGQQKRA SGDPYISHPL EVAAILTDMK
LDESTIAVAL LHDTIEDTTA TRAEIDELFG EDIGRLVEGL TKIKKLDLVT KKAKQAENLR
KLLLAISDDV RVLLVKLADR LHNMRTLDHM SAEKKARISE ETMDIYAPLA GRMGMQDMRE
ELEDLAFRHI NPEAYETVTR RLAEMSQRNE GLIRKIEAEL GELLVAHGLP TAVVRGRQKK
PYSVFRKMQS KSLSFEQLSD VYAFRILVDD APACYRALGI VHTRWRVVPG RFKDYISTPK
QNDYQSIHTT IIGPSRQRIE LQIRTRRMHE IAEYGIAAHA LYKDGESNGN GEKSPPSNAY
ALLRRTIESL AEGDNPEEFL EHTKLELFQD QVFCFTPKGQ LIALPRGATP IDFAYAVHTN
IGDTCVGAKI NGRIMPLVTR LNNGDEVEII RSGIQVPPPA WEEIVVTGKA RAAIRRATRA
AVRKQYSGLG YRILERTFDR AGKSFSRDAL KPVLHRLGHK DVEDSIAAVG RGELSSLDVL
RAVFPDHQDE RVTVKPSQEE GWFPMRSAAG MVFKLPGTSK AQLNAAMGSG PEALPIRGLS
GKAEVHFSEG GAVPGDRIVG IMEKDKGITI YPIQSPSLQK FDDEPERWID VRWDLDEANN
TRFMARIIVN ELNEPGSLAE VTQVLATGDV NIRALTMNRV AADFTEVQMD LEVWDLRQLN
QIISQLKELH CVSTVSRVFT
//
