ID A0A0F4KR55_9LACO Unreviewed; 743 AA.
AC A0A0F4KR55;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:KJY48890.1};
GN ORFNames=JG29_07100 {ECO:0000313|EMBL:KJY48890.1};
OS Bombilactobacillus mellis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1218508 {ECO:0000313|EMBL:KJY48890.1, ECO:0000313|Proteomes:UP000033695};
RN [1] {ECO:0000313|EMBL:KJY48890.1, ECO:0000313|Proteomes:UP000033695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hon2 {ECO:0000313|EMBL:KJY48890.1,
RC ECO:0000313|Proteomes:UP000033695};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (DEC-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:KJY48890.1}.
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DR EMBL; JXBZ01000007; KJY48890.1; -; Genomic_DNA.
DR RefSeq; WP_045922560.1; NZ_KQ033877.1.
DR AlphaFoldDB; A0A0F4KR55; -.
DR STRING; 1218508.JG29_07100; -.
DR PATRIC; fig|1218508.4.peg.728; -.
DR HOGENOM; CLU_012300_3_0_9; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000033695; Unassembled WGS sequence.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000313|EMBL:KJY48890.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000033695};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 50..149
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 393..454
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 669..743
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 559..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 85670 MW; 34F48297A69669D5 CRC64;
MPKEKVYSAQ EVFDICATYM NQRHIDYIKK AYELAAYVHS EQKRASGEPY IVHPIQVAAI
LANLKMDPDT ISAGFLHDVV EDTNIISADI RELFGNDVAT IVEGVTKISK YKYKSHQQLL
AANHRKMLLA TAKDMRVIMV KLADRLHNMR TLNYLRPDKQ RRIANETLEI YAPLADRLGI
STIKWELEDL SLRYLNPQQY YRIVHLMNSK RAQREEYIQA AIREVKVNID QLHIDYDISG
RAKHIYSIYK KMVEKHKQFE ELYDLLAIRI MVNSIRDCYG VLGNIHAQWK PIPGRFKDYI
AVPKVNGYQS LHTTVIGPQG RPLEVQIRTY QMHEVAEYGV AAHWAYKEGK KEKINLDNND
QQIDVFREIM EIQEESSTDA DFMKNIKGDV FSDRVYVFTP KGEVMELPKG AIPLDFAYQV
HTEVGNHTIG AKINGKIVPL DYKLRNGDIV EMLTQSNAAP SRDWENIVYT TRARNKIKRY
FKSVDRQQNI ETGRNKIERE LLDRNFAPKN YLSKKALQPV LERYNFTTED ELLAAVGYGE
VSVIGVVNRL TEAERKKQAQ QKKAEYEEQV MGEASKAAKT KEEHSSEHND NDSETQEREV
HIQGVANLLI HMAKCCTPIP GDEIVGYITK GRGVTIHRQN CPNIQEEDQK ARLIEASWGN
IQNHHYLVKL EIFGFNRNGL LNDILQVVNK QTNMLNDVNG RMDHDRMAHV TLTVGVRNLM
HLKDIMTKIN NIPDVYNVKR VIN
//
