ID A0A1I0M2N9_9BACT Unreviewed; 739 AA.
AC A0A1I0M2N9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SEV82707.1};
GN ORFNames=SAMN05216290_0009 {ECO:0000313|EMBL:SEV82707.1};
OS Roseivirga pacifica.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=1267423 {ECO:0000313|EMBL:SEV82707.1, ECO:0000313|Proteomes:UP000199437};
RN [1] {ECO:0000313|Proteomes:UP000199437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12402 {ECO:0000313|Proteomes:UP000199437};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; FOIR01000001; SEV82707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0M2N9; -.
DR STRING; 1267423.SAMN05216290_0009; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000199437; Unassembled WGS sequence.
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; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:SEV82707.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199437};
KW Transferase {ECO:0000313|EMBL:SEV82707.1}.
FT DOMAIN 402..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 739 AA; 84553 MW; F8673208486762A3 CRC64;
MIAVDLEEER KEIIRRYRKL LRKAKPFLKG DDAKQIKKAF NTSLEAHKEM RRKSGEPYIY
HPIAVAEICV DEIGLGTTSI VAALLHDVVE DTEIELEEIE QDFGPKVAKI IDGLTKISGV
FEHGSSQQAE NFRKMLLTLS DDVRVILIKL ADRLHNMRTL GSMPRHKQLK IISETIYLYA
PLAHRLGLYA IKSELEDLWL KYTEPETYAD IVAKIAESKS SRARFIKSFM NPILEEINKS
GLRYEVKGRP KSIYSIWNKM RKQDIPFEQV YDLFAVRIII DTDYDHEKAA CWQVYSIVTD
FYTPNPDRLR DWVSTPKANG YESLHTTVMS RKGKWVEVQI RTKRMDDIAE KGYAAHWKYK
DGMTPTQESG LEVWIQKVRD MLEQNDTTAI EFVDDFRANL FNEEVFVFTP KGDLKILPVG
ATSLDFAFDI HTEVGAKCLG AKVNNRLVPL NYKLRNGDQV EILTSNKQKP NEDWLRLVVT
SKAKSKIKDT LKEAKKQAAA DGKEIVQRKL KQMKVPFDSD VANQLRAFFE EKTVTDFYYK
VGKGVIDSTE IKKYKDFKTK KSKTVKPAAN STAFSDDFSK IKETGKDILL IGENMDVIDY
RYARCCNPIP GDDVFGFVTI NEGIKIHRTT CPNAPELLSN HGNRIVKAKW LSKQQNAFLA
GLRIIGTDRV GLMRDVTSII SNELKVNMQS ISIDTETGIF DGQIKLYINN TKHLDELIAQ
LEKVTGVMRV TRFESRDDS
//
