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Database: UniProt
Entry: I0INQ5_LEPFC
LinkDB: I0INQ5_LEPFC
Original site: I0INQ5_LEPFC 
ID   I0INQ5_LEPFC            Unreviewed;       751 AA.
AC   I0INQ5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:BAM06904.1};
GN   OrderedLocusNames=LFE_1219 {ECO:0000313|EMBL:BAM06904.1};
OS   Leptospirillum ferrooxidans (strain C2-3).
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM06904.1, ECO:0000313|Proteomes:UP000007382};
RN   [1] {ECO:0000313|EMBL:BAM06904.1, ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|EMBL:BAM06904.1,
RC   ECO:0000313|Proteomes:UP000007382};
RX   PubMed=22815442; DOI=10.1128/JB.00696-12;
RA   Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT   Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT   Japan.";
RL   J. Bacteriol. 194:4122-4123(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA   Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "The complete genome sequence of the pioneer microbe on fresh volcanic
RT   deposit, Leptospirillum ferrooxidans strain C2-3.";
RL   Submitted (MAR-2012) 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   -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; AP012342; BAM06904.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0INQ5; -.
DR   STRING; 1162668.LFE_1219; -.
DR   KEGG; lfc:LFE_1219; -.
DR   PATRIC; fig|1162668.3.peg.1417; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_0; -.
DR   OMA; DWISSPK; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000007382; Chromosome.
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; 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; GTP PYROPHOSPHOKINASE; 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   Kinase {ECO:0000313|EMBL:BAM06904.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007382};
KW   Transferase {ECO:0000313|EMBL:BAM06904.1}.
FT   DOMAIN          68..168
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          411..472
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          665..739
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   751 AA;  85215 MW;  030E5EECC39E4B03 CRC64;
     MNNHDVSDLK ETTVIPISSI VHTVTIDQLI EETSKYNLPE ESQAKIRQAY ELSAKAHEGQ
     FRRSGESYVE HPLNVAWILA SMKVDATCLI TALLHDTLED TTLSSEQIES LFGSKVVSLI
     DGVTKIGKFH FQATKAEKQA ENFRKMLLSM SEDIRVILVK LADRLHNMRT ISSLNIDRQR
     AIAQETLEIY APLANRLGIG WIKSELEDLS FSVQDRETYL DLKVKVSNRR RERKNYISTI
     VKTVQEALIA NNLQGEVQGR YKHIYSIYRK MTIQEIPFEE IYDLMGIRII TDTKLNCYAI
     LGLLHSLWKP MAGRIKDFIA VPKSNMYQSL HTTVIGSEGI PVEFQIRTEE MHRVAEEGIA
     AHWNYKENAD GSPAEGERKV VAWLRQLVEW QKELPDNREF MDSVKVNLFP DEVYVFTPKG
     QVKEMIKGST AIDFAYSIHT ELGHHCMGAR INGRWSPIKT ELQSGDIVEI ISSPSQSPSK
     DWLRFVATPR ARARVRHWLK EEEDRQSAEI GRKSLENEFR KARLNLSDYL KSPYLEVILS
     YSDQPAPTLE NVYSRIGFGQ LSPNVVLRKL VPVTQETPEQ ELPHESFPVS NHPVVVRGGG
     KDLLISLARC CSPVPGEEII GYISRGRGVV IHSRDCPNLV HLSIQKERLI QSTWDNDPNN
     LFEVQIRVLM EDKPGMLAGV SAAISEKGAN INHAEVKQDR HKMAVIEIAL GVKNTSDLES
     IMEAIRRVKG VISVQRLKRM TGENSRRSEP A
//
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