ID ENGB_CAMJR Reviewed; 198 AA. AC Q5HVC1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 02-SEP-2026, entry version 108. DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321}; GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; GN OrderedLocusNames=CJE0753; OS Campylobacter jejuni (strain RM1221). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=195099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM1221; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms from RT the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(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; Evidence={ECO:0000255|HAMAP- CC 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000025; AAW34546.1; -; Genomic_DNA. DR RefSeq; WP_002867727.1; NC_003912.7. DR AlphaFoldDB; Q5HVC1; -. DR SMR; Q5HVC1; -. DR KEGG; cjr:CJE0753; -. DR HOGENOM; CLU_033732_3_2_7; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0090529; P:cell septum assembly; IEA:UniProtKB-UniRule. 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 InterPro; IPR005225; Small_GTP-bd. DR NCBIfam; TIGR03598; GTPase_YsxC; 1. DR NCBIfam; TIGR00231; small_GTP; 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; Septation. FT CHAIN 1..198 FT /note="Probable GTP-binding protein EngB" FT /id="PRO_0000266839" FT DOMAIN 21..195 FT /note="EngB-type G" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321" FT BINDING 29..36 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321" FT BINDING 36 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321" FT BINDING 56..60 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321" FT BINDING 58 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 151..154 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321" FT BINDING 174..176 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321" SQ SEQUENCE 198 AA; 22747 MW; 9313E06B18D59981 CRC64; MIISAKFITS LVKFDENLSS NFSEVAFLGR SNVGKSSLIN SLCKQKNLAK SSATPGKTQL INFFEVICKR NEEKFNINFI DLPGFGYAKV SKNLKEIWNQ NLDEFLKLRT SIKLFIHLID SRHTHLEIDV NLNDYLKRFL RPDQKILKVF TKCDKLNQSE KAKLKNEFKD SILVSNLNKF GLDSLEDIII NQTLGLDK //