ID G7I155_9CORY Unreviewed; 764 AA.
AC G7I155;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Bifunctional GTP diphosphokinase/guanosine-3',5'-bis(Diphosphate) 3'-diphosphatase {ECO:0000313|EMBL:CCE56170.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:CCE56170.1};
DE EC=3.1.7.2 {ECO:0000313|EMBL:CCE56170.1};
GN ORFNames=CCAS_13585 {ECO:0000313|EMBL:CCE56170.1};
OS Corynebacterium casei UCMA 3821.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1110505 {ECO:0000313|EMBL:CCE56170.1, ECO:0000313|Proteomes:UP000004840};
RN [1] {ECO:0000313|EMBL:CCE56170.1, ECO:0000313|Proteomes:UP000004840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCMA 3821 {ECO:0000313|EMBL:CCE56170.1,
RC ECO:0000313|Proteomes:UP000004840};
RX PubMed=22247534; DOI=10.1128/JB.06496-11;
RA Monnet C., Loux V., Bento P., Gibrat J.F., Straub C., Bonnarme P.,
RA Landaud S., Irlinger F.;
RT "Genome Sequence of Corynebacterium casei UCMA 3821, Isolated from a Smear-
RT Ripened Cheese.";
RL J. Bacteriol. 194:738-739(2012).
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:CCE56170.1}.
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DR EMBL; CAFW01000100; CCE56170.1; -; Genomic_DNA.
DR RefSeq; WP_006823604.1; NZ_CAFW01000100.1.
DR AlphaFoldDB; G7I155; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000004840; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase 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; 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 Hydrolase {ECO:0000313|EMBL:CCE56170.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCE56170.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000313|EMBL:CCE56170.1}.
FT DOMAIN 78..175
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 414..479
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 690..764
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 595..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 84574 MW; 7D88C3AF9509E121 CRC64;
MTNNRSTKRP ASSGVRSMSA RLARSLTGGR VKVNPVLDPL LSIHRQFHPR ADVELLNNAY
STAEKLHVGV FRKSGEPYIT HPLAVATIAA EIGMDTTTVV AALLHDTVED TDYSLEDITA
DFGPEVARLV DGVTKLDKVA LGAAAEAETI RKMIVAMAHD PRVLVIKVAD RLHNMRTMRF
LPPEKQAKKA RQTLDVIAPL AHRLGMANVK WELEDLAFAI LYPKKYDEIV RMVADRAPSR
DRALAEIKEQ VSSALKENGI EAEVMGRPKH YWSIYQKMIV RGRDFAEIFD LVGIRILVGD
VNNCYAAIGV VHSLFQALPG RFKDYISSPR FGVYQSLHTT VIAGESTLEV QVRTHEMHYN
AEFGVAAHWR YKEMKGKNSG NNEEVDQMAW MRQLLDWQKE AADPNEFLDS LRYDLTSQQI
FAFTPKGDVV TLPAGSTPVD FAYAVHTEVG HRCIGAKVNG KLVALESELK SGDKVEIFTS
KDANAGPSRD WQEFLVSPRA KAKVRQWFAK ERREEHLEAG RDALATEVQR GGLPMHRLFT
AKSMKQVAEQ LHFEDVDSLY TAIGAGHVSA QHVANQLMAL FGDRDDAADA LASRTPLSEL
ESSRAKQQTE DSKNGSGILV EGSPDVLAKL AKCCQPVPGD EIFGFVTRGG GVSVHRVDCT
NAEKLKSEPE RMMQVEWAQG KSSSGAFAAT LQLEALDRQG LLFEVTKIFS ESKLNVLSMR
SSRGEDHIAT LQFTFSVSDT KQLGALMTTL RNTEGVFDVY RVTA
//
