ENGB_CHLL2
ID ENGB_CHLL2 Reviewed; 192 AA.
AC B3EGV8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, 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=Clim_2197;
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001097; ACD91221.1; -; Genomic_DNA.
DR RefSeq; WP_012467089.1; NC_010803.1.
DR AlphaFoldDB; B3EGV8; -.
DR SMR; B3EGV8; -.
DR STRING; 290315.Clim_2197; -.
DR EnsemblBacteria; ACD91221; ACD91221; Clim_2197.
DR KEGG; cli:Clim_2197; -.
DR eggNOG; COG0218; Bacteria.
DR HOGENOM; CLU_033732_3_0_10; -.
DR OMA; LMMDIRH; -.
DR OrthoDB; 1746051at2; -.
DR Proteomes; UP000008841; 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 PRINTS; PR00326; GTP1OBG.
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..192
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_1000115960"
FT DOMAIN 22..192
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 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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"
FT BINDING 75..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 172..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
SQ SEQUENCE 192 AA; 21383 MW; 8F765C749E7569F2 CRC64;
MKIINAVFYK SVSALTGLPE ETFPEIVFVG RSNVGKSSLL NSLTGVKGLA KTSSTPGKTR
LINYFQINGN IYFVDLPGYG YAAVGHAEKA HWGNLLVSYI EKRRAIALVL VLVDSRHPAM
ASDREMMAFL EYLDRPYGII MTKDDKLTQK ERAAARREME SFSAKAKFIV NYSSFSGKGK
AELLAHFEHY TC