ID ENGB_ECOK1 Reviewed; 215 AA.
AC A1AI47;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=Ecok1_38430;
GN ORFNames=APECO1_2597;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ03337.1; -; Genomic_DNA.
DR AlphaFoldDB; A1AI47; -.
DR SMR; A1AI47; -.
DR KEGG; ecv:APECO1_2597; -.
DR HOGENOM; CLU_033732_1_2_6; -.
DR Proteomes; UP000008216; 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; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03598; GTPase_YsxC; 1.
DR PANTHER; PTHR11649:SF13; ENGB-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11649; MSS1/TRME-RELATED GTP-BINDING PROTEIN; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..215
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_1000205124"
FT DOMAIN 30..204
FT /note="EngB-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 38..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 65..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 83..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 150..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 183..185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
SQ SEQUENCE 215 AA; 24076 MW; 21F27A8F20E05584 CRC64;
METTALTNLN YQQTHFVMSA PDIRHLPSDT GIEVAFAGRS NAGKSSALNT LTNQKSLART
SKTPGRTQLI NLFEVADGKR LVDLPGYGYA EVPEEMKRKW QRALGEYLEK RQSLQGLVVL
MDIRHPLKDL DQQMIEWAVD SNIAVLVLLT KADKLASGAR KAQLNMVREA VLAFNGDVQV
ETFSSLKKQG VDKLRQKLDT WFSEMQPVEE TQDGE
//
