ENGB_THEMA
ID ENGB_THEMA Reviewed; 195 AA.
AC Q9X1H7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=TM_1466;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Necessary for normal cell division and for the maintenance of
CC normal septation. {ECO:0000255|HAMAP-Rule:MF_00321}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00321};
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngB GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00321}.
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DR EMBL; AE000512; AAD36534.1; -; Genomic_DNA.
DR PIR; C72252; C72252.
DR RefSeq; NP_229266.1; NC_000853.1.
DR RefSeq; WP_004081764.1; NZ_CP011107.1.
DR PDB; 3PQC; X-ray; 1.90 A; A/B=1-195.
DR PDB; 3PR1; X-ray; 2.30 A; A=1-195.
DR PDBsum; 3PQC; -.
DR PDBsum; 3PR1; -.
DR AlphaFoldDB; Q9X1H7; -.
DR SMR; Q9X1H7; -.
DR STRING; 243274.THEMA_06980; -.
DR EnsemblBacteria; AAD36534; AAD36534; TM_1466.
DR KEGG; tma:TM1466; -.
DR eggNOG; COG0218; Bacteria.
DR InParanoid; Q9X1H7; -.
DR OMA; LMMDIRH; -.
DR OrthoDB; 1746051at2; -.
DR EvolutionaryTrace; Q9X1H7; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR CDD; cd01876; YihA_EngB; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00321; GTPase_EngB; 1.
DR InterPro; IPR030393; G_ENGB_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR019987; GTP-bd_ribosome_bio_YsxC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03598; GTPase_YsxC; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51706; G_ENGB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..195
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_0000157794"
FT DOMAIN 22..194
FT /note="EngB-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 56..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 74..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 141..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 173..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:3PQC"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3PR1"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3PQC"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:3PQC"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3PQC"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:3PQC"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3PQC"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3PQC"
FT HELIX 85..101
FT /evidence="ECO:0007829|PDB:3PQC"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:3PQC"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:3PQC"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:3PQC"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3PQC"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3PQC"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:3PQC"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3PQC"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:3PQC"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:3PQC"
SQ SEQUENCE 195 AA; 22454 MW; D37A2E1262902FE4 CRC64;
MIIRDVELVK VARTPGDYPP PLKGEVAFVG RSNVGKSSLL NALFNRKIAF VSKTPGKTRS
INFYLVNSKY YFVDLPGYGY AKVSKKERML WKRLVEDYFK NRWSLQMVFL LVDGRIPPQD
SDLMMVEWMK SLNIPFTIVL TKMDKVKMSE RAKKLEEHRK VFSKYGEYTI IPTSSVTGEG
ISELLDLIST LLKEN
