ID   ENGB_LARHH              Reviewed;         222 AA.
AC   C1D5Q6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN   Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=LHK_03095;
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Laribacter.
OX   NCBI_TaxID=557598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9;
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA   Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA   Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO76073.1; -; Genomic_DNA.
DR   RefSeq; WP_012698536.1; NC_012559.1.
DR   AlphaFoldDB; C1D5Q6; -.
DR   SMR; C1D5Q6; -.
DR   STRING; 557598.LHK_03095; -.
DR   EnsemblBacteria; ACO76073; ACO76073; LHK_03095.
DR   KEGG; lhk:LHK_03095; -.
DR   eggNOG; COG0218; Bacteria.
DR   HOGENOM; CLU_033732_1_1_4; -.
DR   OMA; LMMDIRH; -.
DR   OrthoDB; 1746051at2; -.
DR   Proteomes; UP000002010; 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..222
FT                   /note="Probable GTP-binding protein EngB"
FT                   /id="PRO_1000189925"
FT   DOMAIN          22..197
FT                   /note="EngB-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   REGION          201..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT   BINDING         59
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
SQ   SEQUENCE   222 AA;  24981 MW;  2AEFA5D01F440580 CRC64;
     MPLFQNATFF TTVNHLRDLP PTSAEIAFVG RSNAGKSSAI NALANRTRLA YVSKTPGRTQ
     HINFFRLASH FDYFLVDLPG YGYAEVPESV RAHWVELLGR YLQTRESLIG LLLIMDARHP
     LKELDMRMLD FFRMRGQPVH ILLSKSDKMN RQEQNKTLAT VRQALAGYPQ VSIQLFSSSK
     KQGLEQVETV VAGWFAGLEA RQADELTDGE PDDRTPDPDS AS