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Database: UniProt
Entry: B6AZ77_9RHOB
LinkDB: B6AZ77_9RHOB
Original site: B6AZ77_9RHOB 
ID   B6AZ77_9RHOB            Unreviewed;       721 AA.
AC   B6AZ77;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=spoT/relA {ECO:0000313|EMBL:EDZ40968.1};
GN   ORFNames=RB2083_482 {ECO:0000313|EMBL:EDZ40968.1};
OS   Rhodobacteraceae bacterium HTCC2083.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ40968.1, ECO:0000313|Proteomes:UP000005746};
RN   [1] {ECO:0000313|Proteomes:UP000005746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX   PubMed=21036993; DOI=10.1128/JB.01268-10;
RA   Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT   Roseobacter.";
RL   J. Bacteriol. 193:319-320(2011).
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; DS995276; EDZ40968.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6AZ77; -.
DR   STRING; 314270.RB2083_482; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_5; -.
DR   Proteomes; UP000005746; 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:EDZ40968.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005746}.
FT   DOMAIN          44..143
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          381..446
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          626..700
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   721 AA;  80945 MW;  F59E6047098D6162 CRC64;
     MSPDALLATV RTYNPKTNEA LIRTAFEYGE RMHEGQKRHS GEPYFTHPIA VAGILAEQKL
     DDATLITALL HDTIEDTKST YGEVAQMFDE DIAKLVDGVT KLTNLQLSSS ETKQAENFRK
     LFVAMAKDVR VILVKLADRL HNMRTIKAMR PEKQVIKARE TMDIYAPLAG RMGMQWMREE
     LEDLAFRVLN PEGRASIIRR FIRLQRETGD VIEKITGDME KELAAHYIDA TIVGRAKKPY
     SIWRKMEEKE QGFSRLSDIY GFRVITASDE DCYRVLGVIH RRWFAVPGRF KDYISQPKTN
     GYRSIHTTVS GRDGKRVEVQ IRTRQMHDVA EAGVAAHWSY RDGIRSQNPF AVDPVKWVAS
     LNEQFGPEDD HEDFLEAVKL EMYSDQVFCF TPKGEVVKLP RGATPLDFAY AIHTRIGSAC
     VGAKVDGLRV PLWTRLKNGQ SVEIVTAQGQ QPQFTWLDIA ATGKAKSAIR RSLREQDRQR
     FIKLGSELAR SAFENVGRKA TDKALQAAAK TLRLDDSDAM LAELGASLIT ANEVVRAVYP
     ELVEKTDDSI DSNRAVIGLD QDQAHERAQC CQPLPGERII GITQRGRGVV VHAIDCAALS
     QFEDQTHRWV DLHWQAGTHP PIHSAHLDVT IGNDAGVMGR ICTLIGEQGA NISDLAFTDR
     KPDFYRLHLI VDLRDVEHLH SIISVLSAED DVAEVSRHQN PNDANISVTE IGTRLGLQAP
     R
//
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