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Database: UniProt
Entry: B4RN19_NEIG2
LinkDB: B4RN19_NEIG2
Original site: B4RN19_NEIG2 
ID   B4RN19_NEIG2            Unreviewed;       718 AA.
AC   B4RN19;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophophohydrolase {ECO:0000313|EMBL:ACF30186.1};
GN   OrderedLocusNames=NGK_1529 {ECO:0000313|EMBL:ACF30186.1};
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=521006 {ECO:0000313|EMBL:ACF30186.1, ECO:0000313|Proteomes:UP000002564};
RN   [1] {ECO:0000313|EMBL:ACF30186.1, ECO:0000313|Proteomes:UP000002564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945 {ECO:0000313|EMBL:ACF30186.1,
RC   ECO:0000313|Proteomes:UP000002564};
RX   PubMed=18586945; DOI=10.1128/JB.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
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; CP001050; ACF30186.1; -; Genomic_DNA.
DR   RefSeq; WP_003691632.1; NC_011035.1.
DR   AlphaFoldDB; B4RN19; -.
DR   GeneID; 66753511; -.
DR   KEGG; ngk:NGK_1529; -.
DR   HOGENOM; CLU_012300_3_0_4; -.
DR   Proteomes; UP000002564; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase 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   Hydrolase {ECO:0000313|EMBL:ACF30186.1}.
FT   DOMAIN          58..157
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          399..460
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          642..718
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   718 AA;  80159 MW;  2977B3D699563D3A CRC64;
     MPAPQPSAPY DPLTAEARTL LFHTASYLKP EEQAELEKAV AYAFRAHDGQ TRKSGDPYIT
     HPIAVATQLA LWHMDIQGLC AGVMHDVLED TGVTKGEMAA VFGNTVAEMV DGLSKLEKLK
     FEDHAEHQAE SFRKLILAMT KDVRVIVVKL ADRLHNMRTL GSMRPDKRRR IARETLEIYA
     QIANRIGLNN AYRELQDLSF QNLHPNRYET LKKAMDKSRK NRQDVVGKVL RAFGQRLVGA
     NIEAKIKGRE KNLYGIHQKM MAKKLRFAEV MDIYGFRVIV NSIPACYAAL GTLHTLYQPK
     PGRFKDYIAI PKSNGYQSLH TILVGPYGLP IEVQIRTREM DAVAEGGIVG HWSYKSDSKT
     VDQAVLHTNQ WLKNILDLQA SSANAIEFLE HVKVDLFPNE IYILTPKGKI LTLPKGATPV
     DFAYAVHTDI GHKTVAARVN NVMMPLRTKL KTGDSVEIIT SEHAKPNPAW LNFAVSGRAR
     SAIRQYIKNL NRHDAVVLGE SLLQKALSSL LPKDVLLSDG IKEKYLADLN DKQTSFEEVL
     YNVGMGHTLP VYVAMHIAEL AGEHFGSEVR LSSIKVDGQE SGHIHFAECC HPVPGDSIRL
     LLVKGKGMII HRDTCPTLLK SDPEQQLDAD WENMNGQNYR VGLQVQSEDS HGLLALMAQA
     ISDSGADIES VETPSKSQSG TEGFVEFKFL LKVKNLDQLN QIIQNLHSIP YIRKVIRS
//
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