ID A0A161U4J2_9MICO Unreviewed; 754 AA.
AC A0A161U4J2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Bifunctional (P)ppGpp synthase/hydrolase RelA {ECO:0000313|EMBL:KZE90871.1};
GN Name=relA {ECO:0000313|EMBL:KZE90871.1};
GN ORFNames=AVP41_00392 {ECO:0000313|EMBL:KZE90871.1};
OS Microbacterium sp. TNHR37B.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1775956 {ECO:0000313|EMBL:KZE90871.1, ECO:0000313|Proteomes:UP000076535};
RN [1] {ECO:0000313|EMBL:KZE90871.1, ECO:0000313|Proteomes:UP000076535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNHR37B {ECO:0000313|EMBL:KZE90871.1,
RC ECO:0000313|Proteomes:UP000076535};
RA Adelskov J., Patel B.K.;
RT "Draft Genome Sequence of Microbacterium sp. TNHR37B isolated from the
RT Great Artesian Basin of Australia.";
RL Submitted (JAN-2016) 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:KZE90871.1}.
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DR EMBL; LQGV01000001; KZE90871.1; -; Genomic_DNA.
DR RefSeq; WP_067160006.1; NZ_LQGV01000001.1.
DR AlphaFoldDB; A0A161U4J2; -.
DR STRING; 1775956.AVP41_00392; -.
DR PATRIC; fig|1775956.3.peg.396; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000076535; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:KZE90871.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000076535};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 75..172
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 417..478
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 679..753
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 586..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 83545 MW; 5C87EAAB47F059A9 CRC64;
MTETVSSSAQ NPPQSSLRRL VPRLFSRAPS RNGVEQLIRT VRTHHPKGDL AIIERAYQVA
AAAHSSQKRQ SGEPYITHPL AVAQILADLG LGPRAIAAAL LHDTVEDTDY GLDRLRAEFG
DEVAMLVDGV TKLDKVKYGD AAQAETVRKM IVAMSKDIRV LLIKLADRLH NARTWGFVPP
EKAAKKATET LEIYAPLAHR LGIQAIKSEL EDLSFAVLHP KLYVEIDSLV KQRTPQREQY
VQTVIDAVEA DLRDLRIRGR IMGRPKQLYS VYQKMVVRGR EFDDIYDLIG IRVLVGTVRD
CYAVLGAIHA RWTPLPGRFK DYIATPKFNL YQSLHTTVIG PGGRTVEIQI RTNEMHQQAE
YGVAAHWKYK ERVNGGKTGE KALDTDMAWL AHISDWQAET ADPGEFLDSL RFEIGAKEVY
VFTPKGRVIG LPAGGTPVDF AYAVHTEVGH RTMGAKVNGR LVPLESELHS GDVVEVFTSK
NPDAGPSQDW LGFVKSTRAR SKIRGWFTKE RREEAVDQGK DAIARAMRRQ NLPLQRLMSQ
DSFTEVAHQL RYEDVTALYA AVGEGHVSTQ SVIEKVTALV GAQEDTSTGP IDLPPVGRSR
APRGGDSGVL VRGAPDILVK LAKCCTPVPG DEIVGFVTRG SGVSVHRADC TNVRSLKDDP
ERMIEVSWAP TTKSVFLVHI QVEALDRSGL LSDITRVLSE HHVNILSASV QTNNDRLALS
RYVFEMGDIV HLDRVLNAVR RIDAVYDVYR VTSS
//
