RELA_MYCBO
ID RELA_MYCBO Reviewed; 790 AA.
AC P66015; A0A1R3Y1M7; Q50638; X2BLD0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable GTP pyrophosphokinase;
DE EC=2.7.6.5;
DE AltName: Full=(p)ppGpp synthase;
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase;
DE AltName: Full=ppGpp synthase I;
GN Name=relA; OrderedLocusNames=BQ2027_MB2614C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 This enzyme catalyzes the formation of pppGpp which is then hydrolyzed
CC to form ppGpp (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; LT708304; SIU01232.1; -; Genomic_DNA.
DR RefSeq; NP_856260.1; NC_002945.3.
DR RefSeq; WP_003413368.1; NC_002945.4.
DR AlphaFoldDB; P66015; -.
DR SMR; P66015; -.
DR EnsemblBacteria; SIU01232; SIU01232; BQ2027_MB2614C.
DR GeneID; 45426585; -.
DR PATRIC; fig|233413.5.peg.2875; -.
DR OMA; DWISSPK; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; -; 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 Pfam; PF13291; ACT_4; 1.
DR Pfam; PF19296; DUF5913; 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; SSF55021; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00691; spoT_relA; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW ATP-binding; GTP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..790
FT /note="Probable GTP pyrophosphokinase"
FT /id="PRO_0000166552"
FT DOMAIN 105..202
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 450..511
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 714..788
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 87354 MW; 7A7E669241C0E299 CRC64;
MAEDQLTAQA VAPPTEASAA LEPALETPES PVETLKTSIS ASRRVRARLA RRMTAQRSTT
NPVLEPLVAV HREIYPKADL SILQRAYEVA DQRHASQLRQ SGDPYITHPL AVANILAELG
MDTTTLVAAL LHDTVEDTGY TLEALTEEFG EEVGHLVDGV TKLDRVVLGS AAEGETIRKM
ITAMARDPRV LVIKVADRLH NMRTMRFLPP EKQARKARET LEVIAPLAHR LGMASVKWEL
EDLSFAILHP KKYEEIVRLV AGRAPSRDTY LAKVRAEIVN TLTASKIKAT VEGRPKHYWS
IYQKMIVKGR DFDDIHDLVG VRILCDEIRD CYAAVGVVHS LWQPMAGRFK DYIAQPRYGV
YQSLHTTVVG PEGKPLEVQI RTRDMHRTAE YGIAAHWRYK EAKGRNGVLH PHAAAEIDDM
AWMRQLLDWQ REAADPGEFL ESLRYDLAVQ EIFVFTPKGD VITLPTGSTP VDFAYAVHTE
VGHRCIGARV NGRLVALERK LENGEVVEVF TSKAPNAGPS RDWQQFVVSP RAKTKIRQWF
AKERREEALE TGKDAMAREV RRGGLPLQRL VNGESMAAVA RELHYADVSA LYTAIGEGHV
SAKHVVQRLL AELGGIDQAE EELAERSTPA TMPRRPRSTD DVGVSVPGAP GVLTKLAKCC
TPVPGDVIMG FVTRGGGVSV HRTDCTNAAS LQQQAERIIE VLWAPSPSSV FLVAIQVEAL
DRHRLLSDVT RALADEKVNI LSASVTTSGD RVAISRFTFE MGDPKHLGHL LNAVRNVEGV
YDVYRVTSAA
