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OBG_BRAHW
ID   OBG_BRAHW               Reviewed;         680 AA.
AC   C0QX49;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454};
DE   AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN   Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=BHWA1_00207;
OS   Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC   Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX   NCBI_TaxID=565034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49526 / WA1;
RX   PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA   Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA   Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA   Barrero R., Phillips N.D., Hampson D.J.;
RT   "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT   hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT   intestine.";
RL   PLoS ONE 4:E4641-E4641(2009).
CC   -!- FUNCTION: An essential GTPase which binds GTP, GDP and possibly
CC       (p)ppGpp with moderate affinity, with high nucleotide exchange rates
CC       and a fairly low GTP hydrolysis rate. Plays a role in control of the
CC       cell cycle, stress response, ribosome biogenesis and in those bacteria
CC       that undergo differentiation, in morphogenesis control.
CC       {ECO:0000255|HAMAP-Rule:MF_01454}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01454};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}.
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DR   EMBL; CP001357; ACN82707.1; -; Genomic_DNA.
DR   RefSeq; WP_012669760.1; NC_012225.1.
DR   AlphaFoldDB; C0QX49; -.
DR   SMR; C0QX49; -.
DR   STRING; 565034.BHWA1_00207; -.
DR   PRIDE; C0QX49; -.
DR   EnsemblBacteria; ACN82707; ACN82707; BHWA1_00207.
DR   KEGG; bhy:BHWA1_00207; -.
DR   eggNOG; COG0536; Bacteria.
DR   eggNOG; COG0731; Bacteria.
DR   HOGENOM; CLU_025853_0_0_12; -.
DR   OMA; KANEERY; -.
DR   Proteomes; UP000001803; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd01898; Obg; 1.
DR   Gene3D; 2.70.210.12; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01454; GTPase_Obg; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR   InterPro; IPR006074; GTP1-OBG_CS.
DR   InterPro; IPR006169; GTP1_OBG_dom.
DR   InterPro; IPR036726; GTP1_OBG_dom_sf.
DR   InterPro; IPR040084; GTPase_Obg.
DR   InterPro; IPR045086; OBG_GTPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR11702; PTHR11702; 1.
DR   Pfam; PF01018; GTP1_OBG; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDG01083; Uncharacterised_Radical_SAM_Su; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF82051; SSF82051; 1.
DR   TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR   PROSITE; PS51710; G_OBG; 1.
DR   PROSITE; PS00905; GTP1_OBG; 1.
DR   PROSITE; PS51883; OBG; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; GTP-binding; Hydrolase; Iron; Iron-sulfur; Magnesium;
KW   Metal-binding; Nucleotide-binding; S-adenosyl-L-methionine.
FT   CHAIN           1..680
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000386416"
FT   DOMAIN          2..160
FT                   /note="Obg"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT   DOMAIN          161..336
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   DOMAIN          383..613
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   REGION          371..680
FT                   /note="Radical SAM domain"
FT   BINDING         167..174
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         192..196
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         214..217
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         281..284
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         317..319
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         397
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         401
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         404
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
SQ   SEQUENCE   680 AA;  76101 MW;  F81FDAD018F63125 CRC64;
     MDQFIDVVSF EIEAGHGGAG SVSFRREAHV PMGGPDGGNG GDGGDVIVRV DARINSFGKI
     KSRKRFRARD GEPGRARLSD GKRGDDVVIR VPIGTVVYDE DTNNILADLL EDGQSYTVAR
     GGKGGKGNKF YATATNQAPD YAQHGLDGEK LNIRLEVKLI ADIGLVGMPN TGKSSLLARL
     TRANPKIASY PFTTLTPNLG VCYLDYERSF VIADIPGIIE GASEGAGLGL TFLRHIERTG
     ALCFVIDLTD EDVADTYKKL RNELKQYSKE LIKKKSIIVL NKTDMLEKDE IKAKVKAIEK
     AVKKEYKNNK ETHYEEPEIF ALSVFSLDGD MLDKVTNAFY KANEERYDNT KKETKEPLLL
     NQNKTKSKLK TKRVFGPVVS KRLGNSLGID VIPHKTCSYN CIYCQLGSEE NTKTSLANYY
     SVDEIIYELK EALLNNKNID YITFAGSGEP TLYKDLKKLI YEIKQITDIP VCIITNGSLL
     YKQEMRSDLL IADLVIPSLD AGNMDTFKLI DQPNKEIDFD KMVNGLIEFR RVFKGEYWLE
     VFLLKDINDS KEELDDIIKI VNKIKPDRVQ LVTATRRTSN EKAKALNDEE MEKAKKYFEA
     NCSIEIDVPS VSDKAKGNTK KITEEDIINF LIRQPDTVHM IAISFNEDES RVSELLKKLV
     ESGKVREEIV NGVLSYAVNI
 
 
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