ID W0V2V4_9BURK Unreviewed; 719 AA.
AC W0V2V4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:CDG81920.1};
GN ORFNames=GJA_1267 {ECO:0000313|EMBL:CDG81920.1};
OS Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG81920.1, ECO:0000313|Proteomes:UP000027604};
RN [1] {ECO:0000313|EMBL:CDG81920.1, ECO:0000313|Proteomes:UP000027604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA Graupner K., Lackner G., Hertweck C.;
RT "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT agaricidamnosum.";
RL Genome Announc. 3:e00277-e00277(2015).
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 -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; HG322949; CDG81920.1; -; Genomic_DNA.
DR AlphaFoldDB; W0V2V4; -.
DR STRING; 1349767.GJA_1267; -.
DR KEGG; jag:GJA_1267; -.
DR PATRIC; fig|1349767.4.peg.2985; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_4; -.
DR Proteomes; UP000027604; Chromosome I.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000027604}.
FT DOMAIN 53..152
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 394..455
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 644..719
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 719 AA; 80486 MW; 67DEF9A6A7D00F48 CRC64;
MPPSPTAGVA SVSHLADKLS EYLGPADLKK VKEAYRFSDE MHLGQMRRSG EPYISHPIAV
AEICADWKLD AQAIMAALLH DVMEDQDVKK DELIERFGAP VANLVDGLSK LEKIEFQSQI
EAQAENFRKM LLAMASDVRV ILIKLADRLH NMRTLDAMSP VKKRRIAGET MEVYVPIAHR
LGLNNIYREL QDLSFSHLYP MRYRTLAKAV KAARGNRREV VNKILESVKS TLAMAEIGAE
VYGREKTLYG IYKKMRNKHL SFSQVLDVYG FRVVVDSFEN CYVALGTLHS LYKPMPGKFK
DYIAIRKLNG YQSLHTTLIG PYGTPVEFQI RTQEMHRTAE SGVAAHWLYK SGESNMTDLQ
QRTHAWLQSL LDIQQQTGDS AEFLEHVKVD LFPDSVYVFT PKSKIIALPR GATAIDFAYS
IHTGIGDHTV AVKINNETAP LRTELRNGDI VEIVTDSLSR PSPTWLSFVR TGKARSAIRH
HLRTINLPES IILGQQLLTQ ALITLNITPD LPAPLVERLL NESSAKSMDE LHADIGIGKR
MAALVARHIF GLMGGESASV PIDHNSANEL DPVTICGSEG VSVQLAACCL PIPGDQIIGQ
LRRDQGLLVH TSDCSVAKRQ RIKEPDRWIA VRWGTELNRR FDSRIKLLIN NEKGILARVA
AEIGESDANI IYVGMDEDKD HVLDQLRFTI QVKDRVHLAG LLRNVRKVAG VNRILRERS
//
