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ENGB_BURTA
ID   ENGB_BURTA              Reviewed;         219 AA.
AC   Q2SU58;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN   Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=BTH_I3037;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC39144.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000086; ABC39144.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_009888451.1; NZ_CP008786.1.
DR   PDB; 4DHE; X-ray; 2.20 A; A/B=1-219.
DR   PDBsum; 4DHE; -.
DR   AlphaFoldDB; Q2SU58; -.
DR   SMR; Q2SU58; -.
DR   PRIDE; Q2SU58; -.
DR   EnsemblBacteria; ABC39144; ABC39144; BTH_I3037.
DR   KEGG; bte:BTH_I3037; -.
DR   HOGENOM; CLU_033732_1_1_4; -.
DR   OrthoDB; 1746051at2; -.
DR   Proteomes; UP000001930; Chromosome I.
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   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03598; GTPase_YsxC; 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; Septation.
FT   CHAIN           1..219
FT                   /note="Probable GTP-binding protein EngB"
FT                   /id="PRO_0000266837"
FT   DOMAIN          24..207
FT                   /note="EngB-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         32..39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         61
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         81..84
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         148..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         185..188
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   HELIX           1..6
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   STRAND          9..14
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   HELIX           17..19
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   HELIX           35..45
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   STRAND          64..70
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   HELIX           94..108
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   STRAND          112..120
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   HELIX           127..136
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   STRAND          143..148
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   HELIX           155..175
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   STRAND          181..187
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   TURN            188..191
FT                   /evidence="ECO:0007829|PDB:4DHE"
FT   HELIX           194..205
FT                   /evidence="ECO:0007829|PDB:4DHE"
SQ   SEQUENCE   219 AA;  24207 MW;  700149DD587B26AC CRC64;
     MAFLLHQARF FTTVNHLRDL PPTVQPEIAF AGRSNAGKST AINVLCNQKR LAFASKTPGR
     TQHINYFSVG PAAEPVAHLV DLPGYGYAEV PGAAKAHWEQ LLSSYLQTRP QLCGMILMMD
     ARRPLTELDR RMIEWFAPTG KPIHSLLTKC DKLTRQESIN ALRATQKSLD AYRDAGYAGK
     LTVQLFSALK RTGLDDAHAL IESWLRPAAA DEDHAAVAE
 
 
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