ID   ENGB_THIDA              Reviewed;         206 AA.
AC   Q3SMA6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN   Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=Tbd_0188;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ96141.1; -; Genomic_DNA.
DR   RefSeq; WP_011310701.1; NC_007404.1.
DR   AlphaFoldDB; Q3SMA6; -.
DR   SMR; Q3SMA6; -.
DR   STRING; 292415.Tbd_0188; -.
DR   PRIDE; Q3SMA6; -.
DR   EnsemblBacteria; AAZ96141; AAZ96141; Tbd_0188.
DR   KEGG; tbd:Tbd_0188; -.
DR   eggNOG; COG0218; Bacteria.
DR   HOGENOM; CLU_033732_1_0_4; -.
DR   OMA; LMMDIRH; -.
DR   OrthoDB; 1746051at2; -.
DR   Proteomes; UP000008291; Chromosome.
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   3: Inferred from homology;
KW   Cell cycle; Cell division; GTP-binding; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Septation.
FT   CHAIN           1..206
FT                   /note="Probable GTP-binding protein EngB"
FT                   /id="PRO_0000266974"
FT   DOMAIN          25..198
FT                   /note="EngB-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
SQ   SEQUENCE   206 AA;  22769 MW;  2A06E8CE981F4C9A CRC64;
     MTAKPVLNRA HFFTSVAQFR DLPPSRAEVA FAGRSNAGKS SAINLLTRKN RLAFTSKTPG
     RTQLINFFEL TADTYLVDLP GYGYAKVPPE VKAKWEGLLS RYLQEREALA GMVLIMDARH
     PLTPLDRQML EWFAPTGKPV HILLSKADKL SNSEKALTLR KVKQELADRE TVSVQLFSSL
     SRVGAEEAAV RIEGWLAPEA AVHAPG