ID A0A258FNN5_9CAUL Unreviewed; 737 AA.
AC A0A258FNN5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=B7Z01_06480 {ECO:0000313|EMBL:OYX34200.1};
OS Brevundimonas subvibrioides.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=74313 {ECO:0000313|EMBL:OYX34200.1, ECO:0000313|Proteomes:UP000215595};
RN [1] {ECO:0000313|EMBL:OYX34200.1, ECO:0000313|Proteomes:UP000215595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-69-9 {ECO:0000313|EMBL:OYX34200.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYX34200.1}.
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DR EMBL; NCEB01000010; OYX34200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258FNN5; -.
DR Proteomes; UP000215595; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase 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; 2.
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 Hydrolase {ECO:0000313|EMBL:OYX34200.1}.
FT DOMAIN 64..163
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 411..472
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 663..737
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 737 AA; 81504 MW; A76B49E94BEAA79B CRC64;
MANDLASPSD AVPAAKRITV LRQFELIEAV KAYDPTADEA LLNRAYVYAM KMHGSQLRAS
GDPYFAHPIQ VAGILTDYKL DTATIVTALL HDVVEDTSAT RDDIASMFGE EVAVLVEGVT
KLSRLELQAE HTRQAENLRK FILAISRDVR VLLVKLADRL HNMRTLKYVK PEKRERISRE
TLEVYAPLGR SIGIHSIASE LEELAFEHLN PTARTAIERR LEALKLEHGK ATEGVSTEIQ
QVLSEAGIKA RVYGRQKTPY SIWRKLQRKS VGFSSLSDIY GFRVLVEAED DCYRALGVIH
RAWPMVPERF KDFISTPKSN NYRSLHTTVV GPGGLRIEMQ IRTEAMDRVA EDGVAAHWAY
KNTSYGFDQE AMEREGGRDP LQNLRHLVQV IEHGEGGEDW VEHAKLEMYL DQVFVFTPKG
RLITLPQGGM PLDFAYAVHT EVGDTAVGAK INGELKPMRT RLQNGDVVEI IRGKKREAPA
DWRSLTVTGR ARSAIRRHIR SSERDEFQKL GKSTLEQTLG RAGKTLSDVK LTPALETLAL
ATEDDLFDAI GRGRLSANKV AETLFPGLKG TLVTGSDKKK IADDKARLFV RGGGLTPGVS
IHFGECCTPV PGDRIVGILE PEQGLTVHVI DCQRLADFAD DDSVWNDLQW TPQAEQGAVG
MARFRATIQN APGVLGQVAT VIGEAGGNIL NLKMAHRQSD FFDVDLDVEV ADAKHATTIM
AALRANPAVD TVERSRG
//
