ID K1MFE7_9LACO Unreviewed; 746 AA.
AC K1MFE7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=HMPREF9249_01422 {ECO:0000313|EMBL:EKB67900.1};
OS Lactobacillus crispatus FB077-07.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=883092 {ECO:0000313|EMBL:EKB67900.1, ECO:0000313|Proteomes:UP000004722};
RN [1] {ECO:0000313|EMBL:EKB67900.1, ECO:0000313|Proteomes:UP000004722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB077-07 {ECO:0000313|EMBL:EKB67900.1,
RC ECO:0000313|Proteomes:UP000004722};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Lactobacillus crispatus FB077-07.";
RL Submitted (JUL-2012) 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:EKB67900.1}.
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DR EMBL; AGZG01000076; EKB67900.1; -; Genomic_DNA.
DR RefSeq; WP_005729567.1; NZ_JH932273.1.
DR AlphaFoldDB; K1MFE7; -.
DR PATRIC; fig|883092.3.peg.1412; -.
DR HOGENOM; CLU_012300_3_0_9; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000004722; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
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 672..746
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 547..576
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 746 AA; 85460 MW; A43BA411B62469CB CRC64;
MSKYIEMTHD QVIDTCKKYM NDDQVAFVEK AYEFANKAHA GQKRASGQPY IIHPTQVAGT
LATLGLDPDT VAAGFLHDTV EDTPVTNDEL KEKFGEDVAF IVDGVTKLNK YEYKSHQEFL
AENHRKMLIA MAQDLRVIMV KLADRLHNMH TLQHLRPDKQ RRIASETMDI YAPLADRLGI
GTIKWELEDM SFHYLNPEAY YRIVNLMDVK RSQREKYIAD TIKTLKKTLN ELGIKYEIYG
RPKHIYSIYK KMVNKHKDFD EIYDLLAVRV IVKNVRDCYA VLGAVHTEWK PMPGRFKDYI
AMPKVNGYQS LHTTIIGPGG RPLEIQIRTE QMHKVAEYGV AAHWAYKRGN FTGVEQSTSG
EKLDMVREIL ELKDETKDAG EFMKSVKSDI FSDRVYVFTP KGEVYELPKG SVTLDFAYAI
HTQVGSHAVG AKVNNKLVPL DYKLRNGDVI EIMTQTNAAP SRDWVDMVKT SRARNKIRRY
FRSQDREDSI QHGEQLIADM LRDEDLSPKE FMARDRIEKL LEHFNYHTAD ELYAAVGFGD
LSAQAVVNRL TVDLRREEEN QKQKELEEKI LNSGQQAVQE EQPKKNSNTT MKVKHKNGVM
IQGVSDLMLH LAKCCNPVPG DKIIGYVTKG RGVTIHRTDC RNITKEAEEQ GRLIDVEWEN
VEENSVQSFN ANIEVFGYNR SNLLSDVINK LNSLTKNINN ISGKVNEDNV AHMYVTVAVR
DADQLDEILS KLRDIPDVYE TKRSDN
//
