ID D6E7J2_9ACTN Unreviewed; 802 AA.
AC D6E7J2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=(P)ppGpp synthetase, RelA/SpoT family {ECO:0000313|EMBL:CBL03689.1};
GN ORFNames=GPA_09220 {ECO:0000313|EMBL:CBL03689.1};
OS Gordonibacter pamelaeae 7-10-1-b.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL03689.1, ECO:0000313|Proteomes:UP000008805};
RN [1] {ECO:0000313|EMBL:CBL03689.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL03689.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929047; CBL03689.1; -; Genomic_DNA.
DR RefSeq; WP_015539039.1; NC_021021.1.
DR AlphaFoldDB; D6E7J2; -.
DR KEGG; gpa:GPA_09220; -.
DR PATRIC; fig|657308.3.peg.510; -.
DR HOGENOM; CLU_012300_3_0_11; -.
DR BioCyc; GPAM657308:GPA_RS04240-MONOMER; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000008805; Chromosome.
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:UP000008805};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 102..201
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 441..504
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 720..794
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 89783 MW; DCD2EAECBFCD2E6D CRC64;
MGKADHKREE LLGEPLEQAS HKQTVEDDLL GLPHVAQKAF ASEGRADARN PHRTETPEER
FAELQRLTSA YLSEPDQALL AKAFQFASEA HEGQCRKSGE PFVAHPVEVA IILADLRMDV
ETLCAALLHD TVEDTCVTTE QVAVEFNEQV AQLVEGVTKI TRIEVESLSD EQAATIRKMF
VAMSKDIRVI VIKLADRLHN MRTLGALRED RRIFKARETL EIYAPIAHRL GINNIKWELE
DLSFYYLEPN KYKQVSRMVT ESRAEREGYL DQIIGILHDE MEKVGITAQI MGRPKHLYSI
YQKMTQKGKG FSEIYDLIAV RIIVPSVKDC YLALGAVHTL WHPMPGRFKD YIAMPKYNMY
QSLHTTVIGP AGRPLEVQIR TEDMHRQSEY GVAAHWRYKE KGGKSGDAID QQLAWLRQMV
DWQDETQDSR EFLKDLKVDL APSEVFVFTP KGEAMSLRAG STPVDFAYAI HTEVGNHCVG
AKVNGAIVPL TYELQLGDRV EILTQKSASP SRDWLNLVKT PSARSKIRSY FSKVSRGDDL
QNGRDKLTRE MRKHGLGISS AQSMRAVKSV SEHLGYNDPD DMLVNIGTGK ESAQHVANRL
LKILVDKGNE AAETVGLGAG DMSTGKLPPM LTSVKRPKKH EAHSSNGVVV KGIDDVLVRL
SRCCNPVPGD DILGFVTRGR GVSVHRADCP NAQDLMTEPE RIIEVSWENE PSKSTSYQIE
VFVEALDRMN LLRDVAVVLS EVGANVLSSS TTSHRDGMAE MRFLFQVSDI KHIDLILSKL
RGIEGVFDAR RMLPGESGKK KK
//
