ID Q6N6C4_RHOPA Unreviewed; 760 AA.
AC Q6N6C4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=GTP pyrophosphokinase rsh {ECO:0000256|ARBA:ARBA00014315};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
GN Name=relA {ECO:0000313|EMBL:CAE28134.1};
GN OrderedLocusNames=RPA2693 {ECO:0000313|EMBL:CAE28134.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE28134.1, ECO:0000313|Proteomes:UP000001426};
RN [1] {ECO:0000313|EMBL:CAE28134.1, ECO:0000313|Proteomes:UP000001426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426};
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H.,
RA Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; BX572601; CAE28134.1; -; Genomic_DNA.
DR RefSeq; WP_011158243.1; NZ_CP116810.1.
DR AlphaFoldDB; Q6N6C4; -.
DR STRING; 258594.RPA2693; -.
DR GeneID; 66893768; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_5; -.
DR PhylomeDB; Q6N6C4; -.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0016740; F:transferase 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:UP000001426};
KW Transferase {ECO:0000313|EMBL:CAE28134.1}.
FT DOMAIN 79..178
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 423..484
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 686..760
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 84503 MW; DF0303ACE2DD31DB CRC64;
MASGRQGSKQ MEQAGGAAAV AEPTAVAKPR SRARMMRQYD LVERVRSYNP NTDEDLLNRA
YVYAMMAHGE QTRASGDPYF SHPLEVAAIL TNLKLDDATI VAALLHDTIE DTEATRTEID
TMFGPEIGAL VEGLTKLKRL ELVSREAKQA ENLRKLLLAI ADDVRVLLIK LADRLHNMRT
LEFVPPASRQ RIAEETLDIY APLAGRMGMQ EMREELEDLS FRSLDPEAFT VVMQRLDALA
ERNRNLIGEI ESQLSANLAR HGITAEVTGR RKRPFSIWTK MERKSVGFEQ LSDIYGFRVV
LDNVEACYRA LGVVHTTWPM VPGRFKDYIS TPKQNDYRSL HTTVIGPGQQ RVELQFRTRE
MNQIAEYGIA AHAFYKDGVG SPTELLNRES NAFAWLRHTI EMLSESSNPE EFLEHTKLEL
FHDQVFCFTP KGKLIALPRK ANVVDFAYAV HTDVGNSAVG CKINGKFAPL SSELQNGDEV
EVLTSPVQSA PPAAWESLAV TGKARAAIRR ATRVAMRDQY AGLGRRIVER LFARAKIEYA
DDKLKGALPR LARASVEDVM ASVGRGEMKA SDVARAMYPD YKEERIARFG GKKDVPDKVI
GKAPETGKVS SVIPIGGLHS GLPVKFAPNG GAVPGDRIVG IVTPGEGITI YPIQSPDLKE
FEEEPERWLD VKWDIDETTP QRFPARLFVQ NVNEPGSLAQ IAGVIAEHDG NIDNINMSRR
SPDFTELTID LEVYDLKHLS AIIAQLRAKD VVAHVERVNG
//
