ID A0A1S1RBQ0_9ACTN Unreviewed; 857 AA.
AC A0A1S1RBQ0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:OHV43219.1};
GN ORFNames=CC117_11460 {ECO:0000313|EMBL:OHV43219.1};
OS Parafrankia colletiae.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Parafrankia.
OX NCBI_TaxID=573497 {ECO:0000313|EMBL:OHV43219.1, ECO:0000313|Proteomes:UP000179627};
RN [1] {ECO:0000313|Proteomes:UP000179627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc1.17 {ECO:0000313|Proteomes:UP000179627};
RA Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA Nouioui I., Abebe-Akele F., Simpson S., Thomas K., Gtari M., Tisa L.S.,
RA Hurst S.;
RT "Sequence Frankia sp. strain CcI1.17.";
RL Submitted (JUL-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 -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
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:OHV43219.1}.
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DR EMBL; MBLM01000036; OHV43219.1; -; Genomic_DNA.
DR RefSeq; WP_071082793.1; NZ_MBLM01000036.1.
DR AlphaFoldDB; A0A1S1RBQ0; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000179627; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; 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:UP000179627};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 101..198
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 434..499
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 780..854
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 535..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 89632 MW; 740CF25A09634E14 CRC64;
MNAEAAGAGL PAGGFSPALA RADGDVDSRT VAAARQASMR LAHLARRMAA PRTPQVPPEL
RDLVEAHRDF HPKADIAAVI RAYTVADDLH AGQIRRSGDP YISHPLAVAE VLAELGVDTT
TLIAALLHDT VEDTGYSLAA VAEEFNGEVA NLVDGVTKLD KMRFGEAAEA ETLRKLIVAL
ARDYRVLVIK IADRLHNMRT LGFMSEPKQQ KISRVTLEVL APLAHRLGVS VIKRELEDRS
FAVLNPEEHR QISGMVDDFT AAERASGVLG GMVAQLRGAL AEARVGGSVS IRTSHIFSIH
KRAQERGRPP RDYNDIVRVL VLVDDITDCY AALGVIHGMW RPVPGRLRDF VATPKFNMYQ
SLHTSVTDDA GRTVDIQIRT PSMHRLAETG IVAKPVGPGA DGARLEGLSW LHSLLDWQVD
TVDPGEFLES LSSDLNSDEV LTFTPKGKMI ALPARSSPVD VAYAVHTDVG HRAIGARVNG
RLVPLHTRLR NGDVVQILTS NLPGAGPSED WLEFVRTSRA RVRIRKRLAR ARRDAQARAT
QAGAPAVSAV SGVSGASSGG PVARPAGDAG SRGGDQVPPA RATGPHGAVG RPGAPAGIRT
GAGAAVALAN AATAGAVGGG GGATSGRPAV LDGPPTEAGS APVAGTGGTD QTDGAAETGP
ARAGRRARRA GSGRREERPG AAGGTRGRES GGAAATHAST RRGTQNWAGF AEIGGTDVPV
RLARCCLPLP GDTVVGFAGN SSAVSLHRQE CANAAASAAS REQVTVQGWT AAESQTFPTE
IAVEAFDRYG LLADITEVLS DTSASVRAAS TSTSEDRVAH ARFTIEVTGP DQLDRVLAAV
RSVGGVYDCY RACQTTG
//
