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Database: UniProt
Entry: D1BSK4_XYLCX
LinkDB: D1BSK4_XYLCX
Original site: D1BSK4_XYLCX 
ID   D1BSK4_XYLCX            Unreviewed;       781 AA.
AC   D1BSK4;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:ACZ30696.1};
DE            EC=2.7.6.5 {ECO:0000313|EMBL:ACZ30696.1};
GN   OrderedLocusNames=Xcel_1673 {ECO:0000313|EMBL:ACZ30696.1};
OS   Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 /
OS   XIL07).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Xylanimonas.
OX   NCBI_TaxID=446471 {ECO:0000313|EMBL:ACZ30696.1, ECO:0000313|Proteomes:UP000002255};
RN   [1] {ECO:0000313|Proteomes:UP000002255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC   {ECO:0000313|Proteomes:UP000002255};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Foster B., Clum A., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA   Woyke T., Wu D., Gehrich-Schroeter G., Schneider S., Pukall S.R.,
RA   Klenk H.P., Eisen J.A.;
RT   "The complete chromosome of Xylanimonas cellulosilytica DSM 15894.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ30696.1, ECO:0000313|Proteomes:UP000002255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC   {ECO:0000313|Proteomes:UP000002255};
RX   PubMed=21304672; DOI=10.4056/sigs.571102;
RA   Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F.,
RA   Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K.,
RA   Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Xylanimonas cellulosilytica type strain
RT   (XIL07).";
RL   Stand. Genomic Sci. 2:1-8(2010).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC         Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001157};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC       1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; CP001821; ACZ30696.1; -; Genomic_DNA.
DR   RefSeq; WP_012878438.1; NC_013530.1.
DR   AlphaFoldDB; D1BSK4; -.
DR   STRING; 446471.Xcel_1673; -.
DR   KEGG; xce:Xcel_1673; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_11; -.
DR   OMA; DWISSPK; -.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000002255; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002255};
KW   Transferase {ECO:0000313|EMBL:ACZ30696.1}.
FT   DOMAIN          85..182
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          428..491
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          695..769
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   781 AA;  85657 MW;  449B1AFB1D6EBE9A CRC64;
     MSDEVKAARA EGAVGTSAST PSTGIRSRLV RLGVRGGGGV SPALEPLLQA VRAAHPKSDL
     AVIERAYTVA EKAHRGQLRK SGDPYITHPV SVATILAELG FEGTTIAAAL LHDTVEDTDY
     SLDQLRTDFG DDAALLVDGV TKLDKVKYGD AAQAETVRKM VVAMAKDIRV LVIKLADRLH
     NARTWKYVPS SSAERKARET LEIYAPLAHR LGMNTIKWEL EDLSFQALYP KVYDEIVHLV
     AERAPAREEY LSVVREQIQA DLRGAKIKAT VTGRPKHYYS IYQKMIVRGH DFQDIYDLVG
     TRVLVDSVRD CYAALGALHA RWNPVPGRFK DYIAMPKFNM YQSLHTTVVG PGGKPVEIQI
     RTHDMHRRAE YGVAAHWKYK EPAKQGKPGA TPEEQRTNDM AWLRQLVDWQ RETADPSEFL
     DSLRYEIGGA EVYVFTPKGQ VMALPAGSTP VDFAYSVHTE VGHRTMGARV NGRLVPLDSQ
     LQNGDVVDIL TSKAESAGPS RDWLSFVKSA RARNKIRAWF TKERREEAIE HGRDAITKAM
     RKQNLPIQRL LSHETLVGLA TELRFADVSA LYAAVGEGHV SAPHVVELLV KSLGGADGTE
     EDTAEAAVPG VPTTPRRTRT GDPGIVVRGV EDIWVKLAKC CTPVPGDEII GFVTRGAGVS
     VHRADCANVD GLRAQPERIV DVAWSTGSSA TFLVQIQVEA LDRSRLLSDI TRVLSDNHVN
     ILSASVSTTQ DRIAMSRYVF EMAEPAHLAQ VLSAVRKVDG VFDVYRITGA KAAAAPHLPP
     L
//
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