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Database: UniProt
Entry: A0A069RH56_PEPLI
LinkDB: A0A069RH56_PEPLI
Original site: A0A069RH56_PEPLI 
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
//
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