ID A0A0G3H2K4_9CORY Unreviewed; 777 AA.
AC A0A0G3H2K4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=(P)ppGpp synthetase, RelA/SpoT family {ECO:0000313|EMBL:AKK06068.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:AKK06068.1};
GN Name=relA {ECO:0000313|EMBL:AKK06068.1};
GN ORFNames=CMUST_08720 {ECO:0000313|EMBL:AKK06068.1};
OS Corynebacterium mustelae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK06068.1, ECO:0000313|Proteomes:UP000035199};
RN [1] {ECO:0000313|EMBL:AKK06068.1, ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK06068.1,
RC ECO:0000313|Proteomes:UP000035199};
RX PubMed=26358597;
RA Ruckert C., Eimer J., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT 45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL Genome Announc. 3:e01012-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT from various tissues of a male ferret with lethal sepsis.";
RL Submitted (MAY-2015) 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}.
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DR EMBL; CP011542; AKK06068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3H2K4; -.
DR STRING; 571915.CMUST_08720; -.
DR KEGG; cmv:CMUST_08720; -.
DR PATRIC; fig|571915.4.peg.1853; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000035199; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000035199};
KW Transferase {ECO:0000313|EMBL:AKK06068.1}.
FT DOMAIN 93..190
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 434..495
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 701..775
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 777 AA; 86166 MW; CBCC7E225050B604 CRC64;
MEKALKLKLT LLLKGVNMTQ QRTMKQSSTM RSMSARLARS LTGNRGKINP VLEPLLSIHR
EFHPKADVDA LSRAYDTAER LHKGVFRKSG DPYITHPLAV ATIAAEIGMD TTTLIAALLH
DTVEDCDYSL EELTEDFGEE VARLVDGVTK LDKVALGAAA EAETIRKMIV AMAHDPRVLV
IKVADRLHNM RTMRFLPPEK QAKKARQTLE VIAPLAHRLG MASVKWELED LSFAILYPKK
YDEVVRLVAD RAPSRDRYLK EITAILQQGL KENNIDAEVM GRPKHYWSIY QKMIVRGKDF
DEIFDLVGIR ILVDSLNNCY AAIGVVHSLF AAMPGRFKDY ISSPKFGVYQ SLHTTVMGDG
GKPLEVQVRT HEMHFNAEYG IAAHWRYKET KGSHSGEQAE VDQMAWMRQL LDWQKEAADP
NEFLDSLRYD LTSKQIFVFT PKGDVVNLPM DATPIDFAYA VHTEVGHRCI GAKINGKLVA
LESTLKSGDR VEIFTSKDPN AGPSRDWQDF VRSPRAKAKI RQWFAKERRE EYLEAGRDAL
AAEVQRGGLP IHRLFTAQSM KAVAAELHYA DVDALYTAIG SSAVSAAHVA NRLMAAFGDA
DDAADTLVAR TPFSELVNAK HKAVADGTGI LVEGSPDVMA KLAKCCMPVP GDAIFGFVTR
GGGVSVHRTD CTNAEKLAEE PERMINVSWA SEGHGSVFQA TLQLEALDRN GLLMELTRVI
NEQQVSVVAM NSHSSEDHVA TVRFTFTVSD TKQLGSLMTQ LRNTEGVFDV YRVTSGG
//
