ID A0A1I2DIH5_9RHOB Unreviewed; 712 AA.
AC A0A1I2DIH5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN04488523_110173 {ECO:0000313|EMBL:SFE80277.1};
OS Sulfitobacter brevis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=74348 {ECO:0000313|EMBL:SFE80277.1, ECO:0000313|Proteomes:UP000198977};
RN [1] {ECO:0000313|EMBL:SFE80277.1, ECO:0000313|Proteomes:UP000198977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11443 {ECO:0000313|EMBL:SFE80277.1,
RC ECO:0000313|Proteomes:UP000198977};
RA de Groot N.N.;
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; FOMW01000010; SFE80277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2DIH5; -.
DR STRING; 74348.SAMN04488523_110173; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000198977; 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; 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:SFE80277.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198977}.
FT DOMAIN 49..148
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 390..451
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 631..705
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 712 AA; 80174 MW; FF2CA67864C7E88C CRC64;
MTYAETTADD LVALVRSYNP KTNEPLIRRA YDYGAKMHDG QFRHSGEPYF SHPVAVAVLL
TEQRLDDATI ITALLHDTIE DTRASYSEVE TLFSHEVAEL VDGVTKLTNL QLNSTETKQA
ENFRKLFMAM SKDLRVILVK LADRLHNMRT IKSMRPDKQT QKARETMDIY APLAGRMGMQ
WMREELEDLA FRVLNPEGRA SIIRRFITLQ RESGDVIQRI TGDMRGELAK VGIEAEVIGR
AKKPYSIWRK MEEKAQSFSR LSDIYGFRVI TESDEDTYRT LGAIHQRWRA VPGRFKDYIS
QPKSNGYRSI HTTVSGRDGK RVEVQIRTRQ MHDVAETGVA AHWSYRDGVR SKNPFAVDPA
KWIAQLTEQF DAEDDHEDFL EAVKLEMYAD QVFCFTPKGD VVKLPRGATP IDFAYAIHTR
IGNACVGAKI DGMRVPLWTR VKNGQSIEII TAQGQTPQAT WLDIATTGKA KSAIRRSLRE
VDRERFIKLG RELARSAFAH VGKKATEKAL STAARNMRLD GVDDVLARLG SSEVTGRAVV
QSVYPDLAPR KSDQIDSEHA VVGLEPGQSF DRAPCCNPLP GERIVGIAFR GRGVTVHAID
CERLSTYEDQ PDRWLDLRWH EGNHPAVYSA VFDITLGNGA GVLGRICTLI GEASANIADL
EFLERRPDFY RLLIYVELRD VAHLHSLMLT LEAESDVAAI SRHRDPSAGK PH
//
