ID Q6MTD3_MYCMS Unreviewed; 750 AA.
AC Q6MTD3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=GTP diphosphokinase {ECO:0000313|EMBL:CAE77103.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:CAE77103.1};
GN Name=relA {ECO:0000313|EMBL:CAE77103.1};
GN OrderedLocusNames=MSC_0475 {ECO:0000313|EMBL:CAE77103.1};
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632 {ECO:0000313|EMBL:CAE77103.1, ECO:0000313|Proteomes:UP000001016};
RN [1] {ECO:0000313|EMBL:CAE77103.1, ECO:0000313|Proteomes:UP000001016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1 {ECO:0000313|EMBL:CAE77103.1,
RC ECO:0000313|Proteomes:UP000001016};
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
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}.
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DR EMBL; BX293980; CAE77103.1; -; Genomic_DNA.
DR RefSeq; NP_975461.1; NC_005364.2.
DR AlphaFoldDB; Q6MTD3; -.
DR STRING; 272632.MSC_0475; -.
DR KEGG; mmy:MSC_0475; -.
DR PATRIC; fig|272632.4.peg.515; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_14; -.
DR Proteomes; UP000001016; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000001016};
KW Transferase {ECO:0000313|EMBL:CAE77103.1}.
FT DOMAIN 60..159
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 405..468
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 674..749
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 492..527
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 750 AA; 86650 MW; E4BC94E3D9458FAB CRC64;
MHNKYNYISF DYREIKDFKD LLNELKKYIK NKSELERIEQ AYKYAFKCHF NQTRKNGDPY
IYHPLSAAYY LAQWRMGPNT IIAGLLHDIL EDTPIQKEEL VELFNEEVAN LVESVTKVSF
FAKENRQQIK SKYLRKLYLS MSKDIRVIII KIADRLHNIY TIKNLRSEKQ KIIAQETLEI
YSAIAHRIGM KSAKSLLEDR SFEILNPQEF KKITDLFNSD MQNRQQIIND IIINLEQYLK
KEKNIKIISI FGRPKTIYSI YRKMNVIGKN FEEISDLLAI RIIAKSIDDC YKILGFIHQK
YIPLAGKFKD YIATPKNNVY QSLHTTLSDA NGNIFEVQIR TEEMNQVAET GAAAHWRYKE
GEIIDIAKKQ KEIDEKIDIF SRILDLDKSE DQQSSIEQSI KDDLFTASIY VLTPNGAVIT
LPYGSTVLDF AYRIHTEIGE KTIGARVDGV FLPINTVLKS GEVVEVKTSP KQEPTHEWLK
IVVISNARNR IKKYLQKKIN EETLDKKDQQ KELIRKTEAN INAYINQKDW KWKKKTADEI
LETVKTMDYN SLNDFLLDVA KGEFTINEAA EKVFIKQNYS KDDEAYASIK SKIIYDTTIK
NDILVDGIKN IKTTLASCCM PIPYEEVVGF VTKNNGIKVH LKECINIDWT NMKSRLVVVQ
WNEAVAEKNT YTTKLKYFGI DRNKLLYDIS KIISGLKVSI INANIFTDEK SLLSSGVITI
KIKNSNQLTQ TISALRSIPG INGVERGISN
//
