ID K0YK56_9ACTN Unreviewed; 788 AA.
AC K0YK56;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:EJZ83881.1};
GN ORFNames=HMPREF9451_01403 {ECO:0000313|EMBL:EJZ83881.1};
OS Slackia piriformis YIT 12062.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Slackia.
OX NCBI_TaxID=742818 {ECO:0000313|EMBL:EJZ83881.1, ECO:0000313|Proteomes:UP000006069};
RN [1] {ECO:0000313|EMBL:EJZ83881.1, ECO:0000313|Proteomes:UP000006069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12062 {ECO:0000313|EMBL:EJZ83881.1,
RC ECO:0000313|Proteomes:UP000006069};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Slackia piriformis YIT 12062.";
RL Submitted (AUG-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 -!- 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:EJZ83881.1}.
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DR EMBL; ADMD01000007; EJZ83881.1; -; Genomic_DNA.
DR RefSeq; WP_009139600.1; NZ_JH815198.1.
DR AlphaFoldDB; K0YK56; -.
DR PATRIC; fig|742818.3.peg.1480; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR InParanoid; K0YK56; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000006069; Unassembled WGS sequence.
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:UP000006069};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 91..190
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 430..493
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 706..780
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 788 AA; 87897 MW; 0A594129B50A3F98 CRC64;
MSDEKNASQV GAPIDPVLAR ASGAWAFEIY EGGIAPSAKP SEARAPEVRF AKLQGVTAEY
INEDDQALLE KAYRFASEAH KEQKRKSGEP FIAHPIEVAL ILADLRMDAD TLCAALLHDT
VEDTPTTVEE VSELFNPQVA QLVQGVTKIT RIEVGSLTDE QAATIRKMFV AMSKDIRVIV
IKLADRLHNM RTLSALKEDR RIFKARETLE IYAPIAHRLG IGSIKWELED LSFYYLDPAK
FGQISRMVAE SRVERERYLA DVIETLTGEL TKVNITGHIA GRPKHLYSIY QKMTKRGKGF
SEIYDLIAVR VIVKTVKDCY SVLGAVHALW HPMPGRFKDY IAMPKLNMYQ SLHTTVIGPS
GRPLEVQIRT EEMHRMSEYG VAAHWRYKEK GSKADEAFDR QIAWLRQMVD WQEETKDSRE
FLSDLKVDLA PTEVFVFTPA GDVMSLRSGS TPVDFAYNVH SEVGNHCVGA KVNGAIVPLS
YELQMGDRVE ILTQKSATPS RDWIKMVKTP SARSKLRSYF SKVSRSDDLI QGRDKLAREM
KKHGFGLGST SSVRAQKSVA EQMGYKDVED MMVAIGAGKE TVLHVANRLL KILNPQPVND
TPSIPMMSSG VMPPLITSVK RPNVRRKAHA SNGVIVAGLE NAPVRLSRCC NPVPGDAIIG
FVTRGRGVSV HRADCPNAKD LMRDQGRLIK VEWEATAETT SSYQVEVFIE ALDRMNLLRD
IINTLSDTGV NVLASNTVSH SDGIVEMRYL FQVSQVSHIE NILESLLRID GVFDARRMLP
GDAAHKKK
//
