RELA_CORGL
ID RELA_CORGL Reviewed; 760 AA.
AC O87331;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=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; Synonyms=rel; OrderedLocusNames=Cgl1653, cg1861;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=9695918; DOI=10.1099/00221287-144-7-1853;
RA Wehmeier L., Schaefer A., Burkovski A., Kraemer R., Mechold U., Malke H.,
RA Puehler A., Kalinowski J.;
RT "The role of the Corynebacterium glutamicum rel gene in (p)ppGpp
RT metabolism.";
RL Microbiology 144:1853-1862(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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. It also has (p)ppGpp-degrading activities.
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; AF038651; AAC35494.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99046.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20036.1; -; Genomic_DNA.
DR RefSeq; NP_600866.1; NC_003450.3.
DR RefSeq; WP_003855910.1; NC_003450.3.
DR RefSeq; WP_011265777.1; NC_006958.1.
DR AlphaFoldDB; O87331; -.
DR SMR; O87331; -.
DR STRING; 196627.cg1861; -.
DR PRIDE; O87331; -.
DR GeneID; 58309164; -.
DR KEGG; cgb:cg1861; -.
DR KEGG; cgl:Cgl1653; -.
DR PATRIC; fig|196627.13.peg.1614; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR OMA; DWISSPK; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000000582; 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..760
FT /note="GTP pyrophosphokinase"
FT /id="PRO_0000166545"
FT DOMAIN 77..174
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 418..479
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 684..758
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT CONFLICT 262
FT /note="E -> G (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 84447 MW; 1A72E595DE85E073 CRC64;
MSLERNTQKS SMGVRSMSAR LARSLTGNRV RTNPVLDPLL SIHRQFHPRA DVQVLERAYD
TAERLHDGVI RKSGDPYITH PLAVATIAAE IGMDTTTLVA ALLHDTVEDT DYSLDDLTRD
FGEEVARLVD GVTKLDKVAL GAAAEAETIR KMIVAMSQDP RVLVIKVADR LHNMRTMRFL
PPEKQAKKAR QTLEVIAPLA HRLGMASVKW ELEDLSFAIL YPKKYEEIVR LVADRAPSRD
RYLKEIIDQV TGGLRENNIA AEVLGRPKHY WSIYQKMIVR GRDFDDIFDL VGIRILVDNV
NNCYAAIGVV HSLFNALPGR FKDYISAPRF GVYQSLHTTV MGPGGKPLEV QARTHDMHYN
AEFGIAAHWR YKETKGSHSG EQAEVDQMAW MRQLLDWQKE AADPNEFLDS LRYDLTSKQI
FVFTPKGDVV NLPVNSTPVD FAYAVHTEVG HRCIGAKING KLVALETKLK SGDRVEVFTS
KDQNAGPSRG WQEFVVSPRA KAKIRQWFAK ERREEYLEAG RDALAAVIQR GGLPMHRLFT
ASSMKTVATE LHYPDVDALY TAIGSGSVSA QHVVNRLMAI FGDEEDAEDA LVARTPFSEL
VNSRATTESS TGILVEGSPD VMAKLAKCCM PVPGDEIFGF VTRGGGVSVH RTDCTNVEKL
KEEPERIVSV SWASEGQGSV FSATLQLEAL DRAGLLFELT RVINEQKVSV TAMNSHCSED
RVATVRFTFA VSDTKQLGSL MTQLRNAEGV FDVYRVTSGG
