ID C2ES93_9LACO Unreviewed; 750 AA.
AC C2ES93;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
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:EEJ41285.1};
GN ORFNames=HMPREF0549_0329 {ECO:0000313|EMBL:EEJ41285.1};
OS Limosilactobacillus vaginalis DSM 5837 = ATCC 49540.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423814 {ECO:0000313|EMBL:EEJ41285.1, ECO:0000313|Proteomes:UP000004483};
RN [1] {ECO:0000313|EMBL:EEJ41285.1, ECO:0000313|Proteomes:UP000004483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49540 {ECO:0000313|EMBL:EEJ41285.1,
RC ECO:0000313|Proteomes:UP000004483};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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:EEJ41285.1}.
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DR EMBL; ACGV01000021; EEJ41285.1; -; Genomic_DNA.
DR AlphaFoldDB; C2ES93; -.
DR STRING; 1423814.HMPREF0549_0329; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000004483; 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: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; 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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000313|EMBL:EEJ41285.1}.
FT DOMAIN 55..154
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 400..461
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT REGION 563..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 85114 MW; CD1E6BB83CD490B3 CRC64;
MEGGTLSEVK ELSHEDVLKM VSSYMNDEHV ALVERAYHFA AVCHRDQRRK SGEPYIIHPI
QVAGILADLH MDPETVCAGY LHDIVEDTGA TLDDIKELFG PTIALIVDGD TKLGKIQYKS
NKEQMAATHR KLLLAMSKDI RVMIVKLADR LHNMRTLQHL RPDKQRRISN ETLEIYAPIA
DRLGISTIKW ELEDLSLRYL NPQQYYRIVH LMNSRRDQRV EYIDEAIGEI KKAISDLNLG
PNVEIYGRPK HIYSIYRKMV NQHKQFSQIY DLLAVRIVVD SIKDCYAALG AIHTNWKPMP
GRFKDYIAMP KANGYQSLHT TIMGPGGKPL EVQIRTHHMH QVAEYGVAAH WAYKEGKTNG
IQQTRDSQKL NVVKEILELR SESDGTDEFM QGVQSDIFAD KVYAFTPKGD VIELPQGSGP
LDMAYQIHTE VGNHTTGAKV NGRIVPLDYE IKTGDIVDIL TSSSSAGPSR DWLELVSTRR
ARNKIRQFFR AHDRETNIEE GKRMIEREIR EAGFDPFTLM TEEKNEEVAN QMHYQSSDDM
FAAIGFGDMA PVGVRNRFTA DVRKKEEDSR KQAAEKAVLE EHATLEKPDQ REKKKQAKET
SEGIIVEGVD NLLTRLSHCC SPVPGDDIVG YITKGRGVSV HRSDCPNIKA AEKSGQRIIH
VYWANPNGDK TNYNSNIEVQ GYNRSGLLND VLRSVNNTTK FLNSVNGKVD HNKMVTISMT
IGVRNLHQLQ FIMDSLKNIK DVYVVKRTIR
//
