ID A0A069RH56_PEPLI Unreviewed; 727 AA.
AC A0A069RH56;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN Name=relA {ECO:0000313|EMBL:KDR96093.1};
GN ORFNames=CLIT_5c01050 {ECO:0000313|EMBL:KDR96093.1};
OS Peptoclostridium litorale DSM 5388.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoclostridium.
OX NCBI_TaxID=1121324 {ECO:0000313|EMBL:KDR96093.1, ECO:0000313|Proteomes:UP000027946};
RN [1] {ECO:0000313|EMBL:KDR96093.1, ECO:0000313|Proteomes:UP000027946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W6 {ECO:0000313|EMBL:KDR96093.1,
RC ECO:0000313|Proteomes:UP000027946};
RA Poehlein A., Jagirdar A., Khonsari B., Chibani C.M.,
RA Gutierrez Gutierrez D.A., Davydova E., Alghaithi H.S., Nair K.P.,
RA Dhamotharan K., Chandran L., G W., Daniel R.;
RT "Genome sequence of Clostridium litorale W6, DSM 5388.";
RL Submitted (MAR-2014) 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 -!- 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 Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
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:KDR96093.1}.
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DR EMBL; JJMM01000005; KDR96093.1; -; Genomic_DNA.
DR RefSeq; WP_038262688.1; NZ_JJMM01000005.1.
DR AlphaFoldDB; A0A069RH56; -.
DR STRING; 1121324.CLIT_5c01050; -.
DR eggNOG; COG0317; Bacteria.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000027946; Unassembled WGS sequence.
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; 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; GTP PYROPHOSPHOKINASE; 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 Kinase {ECO:0000313|EMBL:KDR96093.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027946};
KW Transferase {ECO:0000313|EMBL:KDR96093.1}.
FT DOMAIN 43..142
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 385..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 653..727
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 727 AA; 82850 MW; E7D4D42D29929D85 CRC64;
MLENLLLSIE QYSPDSDLEL IIKAYNLAES AHVGQYRKSG ERYFVHPVSV AKILVELQMD
VMTIAAGLLH DVVEDTKYTY DDIKKLFGTE VAELVDGVTK LGKIEYKSKE ETQAENIRKM
FIAMAKDIRV VLIKLADRLH NMRTLNYMSE AKAKEKARET LEIYAPIANR LGISKIKFEL
EDTALRYLDP DGYYELVEKV SKKKRQREDY IQNVIKLLKE NVEDLGVEFE ISGRAKHFYS
IYRKMHYQGK GFDQIYDLTG VRIIVNSIKD CYAILGVVHT IWRPIPGRFK DYIAMPKPNM
YQSIHTTVVG LDGGPLEIQV RTFDMHKTAE YGIAAHWQYK EGKTGMDKDD LDKKLSWLRQ
MMEWQDDLND PREFMEALKI DLFTNQVFVF TPKGDVIEMP AGSTPIDFAY KVHTDVGNKC
IGAKIDGRMV PIDYKLKNGN IVQVVTSSSS SGPSRDWLNI AKSSHAKNKI KQWFRKANRS
ENIEKGKELL FQEAKRHGLS ASEIFKHKYM SLVLKKLNYS NEEELHAAIG YGGITANQVI
GKLKFELEKD TVKDDAKRDA EIMGRIQEKE QKPKEKTRSQ GIVVKGVDNI LVRFAKCCNP
LPGDDIIGFI TKGRGVSIHR KDCPNINIED PESINRIIDV EWDLKKKASF EAEVKVKAND
RSGLLTEITQ IFVSEKISLN GINARTGKDG IANMTLLLQV ESKEQLKSIM NKIKSLSGVL
DVFRVVN
//