RELA_MYCLE
ID RELA_MYCLE Reviewed; 787 AA.
AC Q49640;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=ML0491; ORFNames=B1177_C1_168, MLCB1259.09;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; U00011; AAA17089.1; -; Genomic_DNA.
DR EMBL; AL023591; CAA19084.1; -; Genomic_DNA.
DR EMBL; AL583918; CAC29999.1; -; Genomic_DNA.
DR PIR; S72725; S72725.
DR RefSeq; NP_301430.1; NC_002677.1.
DR RefSeq; WP_010907754.1; NC_002677.1.
DR AlphaFoldDB; Q49640; -.
DR SMR; Q49640; -.
DR STRING; 272631.ML0491; -.
DR EnsemblBacteria; CAC29999; CAC29999; CAC29999.
DR KEGG; mle:ML0491; -.
DR PATRIC; fig|272631.5.peg.855; -.
DR Leproma; ML0491; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR OMA; DWISSPK; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000000806; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..787
FT /note="Probable GTP pyrophosphokinase"
FT /id="PRO_0000166550"
FT DOMAIN 102..199
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 447..508
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 711..785
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 87266 MW; DE2EB784AA9EF061 CRC64;
MADDQGTAQA LQPVQVVPGP AVEAPETPVE TLKTSSSASR RVRARLARRM TAQRSTISPV
LEPLVAVHKE FYPKANLSIV QRAFEVADQR HASQLRRSGD PYITHPLAVA NILAELGMDI
TTLVAALLHD TVEDTGYTLE ALSEEFGDEV GHLVDGVTKL DRVVLGSAAE GETIRKMITA
MARDPRVLVI KVADRLHNMR TMRFLPPEKQ ARKARETLEV IAPLAHRLGM ASVKWELEDL
SFAILHPKKY EEIVRLVAGR APSRDTYLAK VRAEIISTLG ASKIKATVEG RPKHYWSIYQ
KMIVKGRDFD DIHDLVGIRI LCDEIRDCYA AVGVVHSLWQ PMAGRFKDYI AQPRYGVYQS
LHTTVVGPEG KPLEVQIRTR DMHRTAEYGI AAHWRYKEAK GRNGVLHPHA AAEIDDMAWM
RQLLDWQREA AEPGEFLESL RYDLAVQEIF VFTPKGDVIT LPTGSTPVDF AYAVHTEVGH
RCIGARVNGR LVALERKLEN GEFVEIFTSK APNAGPSRDW QQFVVSPRAK TKIRQWFAKE
RREEALEAGK DAMAREVRRG GLPLQRLVNG ESMAAVAREL HYIDVSALYT AIGEGHVSAR
HVVQRLLAEL GGIDQAEEEL AERSTPTTML RRQRSTDDVG VSVPGAPGVL TKLAKCCTPV
PGDAIMGFVT RGGGVSVHRT DCTNTASLQQ QAERIIEVLW APSSSSVFLV AIQVEALDRH
RLLLDITRAL ADERVDILSA SVTTSGDRVA ISRFTFEMGD PKHLGHLLNV VRNVEGVYDV
YRVMSAS
