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Database: UniProt
Entry: K9DE42_9BURK
LinkDB: K9DE42_9BURK
Original site: K9DE42_9BURK 
ID   K9DE42_9BURK            Unreviewed;       747 AA.
AC   K9DE42;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:EKU82929.1};
GN   ORFNames=HMPREF9710_01940 {ECO:0000313|EMBL:EKU82929.1};
OS   Massilia timonae CCUG 45783.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU82929.1, ECO:0000313|Proteomes:UP000009874};
RN   [1] {ECO:0000313|EMBL:EKU82929.1, ECO:0000313|Proteomes:UP000009874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU82929.1,
RC   ECO:0000313|Proteomes:UP000009874};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Massilia timonae CCUG 45783.";
RL   Submitted (SEP-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   -!- 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:EKU82929.1}.
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DR   EMBL; AGZI01000021; EKU82929.1; -; Genomic_DNA.
DR   RefSeq; WP_005665921.1; NZ_JH992922.1.
DR   AlphaFoldDB; K9DE42; -.
DR   STRING; 47229.LO55_2525; -.
DR   GeneID; 84812125; -.
DR   PATRIC; fig|883126.3.peg.1972; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_4; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000009874; Unassembled WGS sequence.
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:UP000009874}.
FT   DOMAIN          80..179
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          421..482
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          672..747
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   747 AA;  83941 MW;  45AA58349CA08922 CRC64;
     MNLSPDSTNT RNPAAPRERR ADNRPPDYLE PVAPGVASVT QLITMLSEYL TPAELKKVKE
     AYRFSDEMHL GQVRKSGEPY ISHPIAVAEI CAEWKLDAQA IMAALLHDVI EDQDVKKDEL
     IERFGAQVAN LVDGLSKLEK IEFQSQLEAQ AENFRKMLLA MASDVRVILI KLADRLHNMR
     TLGVMVPAKK RRIAGETMEV YVPIAHRLGL NNIYRELQDL SFSHLYPLRY QTLSKAIKAA
     RGNRREVVKK ILEAVKNQLA TSGLQFEVYG REKTLYGIYK KMRNKHLSFS QVLDVYGFRV
     VVDSVPNCYV ALGTLHALYK PMPGKFKDYI AIGKINGYQS LHTTLIGPYG TPVEFQIRTQ
     EMHRTAESGV AAHWLYKTGD SNMSDLQQRT HAWLQSLLDI QQQTGDSAEF LEHVKVDLFP
     DSVYVFTPKS KIIALPRGAT ALDFAYSIHT GIGDHTVGVK INNEDQPLRT ELHNGDIVEI
     ITDPESRPSP TWLTFVRTGK ARSAIRHHLR AIDVNESVDL GQELLAQALA VRNIKPDLSD
     AVIERLLAET SAKSMEEMYA DIGIGKRMPA LVARHIFGLM EGDPELLPSS KPLPASEIAP
     VTIYGSEGVA VQLAPCCLPI PGDQITGQLR RDQALVVHTC DCLPAKRIRA KEPDRWIAVQ
     WGDELNRRFD CRIRLLINNE KGILARVAAE IGESDANITY VGMDEDDEHS MTQLRFTIQI
     KDRVHLAQLI RNLRRVAGVN RVERERS
//
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