ENGB_ALKOO
ID ENGB_ALKOO Reviewed; 208 AA.
AC A8MIS4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=Clos_2170;
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) 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; CP000853; ABW19706.1; -; Genomic_DNA.
DR RefSeq; WP_012160015.1; NC_009922.1.
DR AlphaFoldDB; A8MIS4; -.
DR SMR; A8MIS4; -.
DR STRING; 350688.Clos_2170; -.
DR EnsemblBacteria; ABW19706; ABW19706; Clos_2170.
DR KEGG; aoe:Clos_2170; -.
DR eggNOG; COG0218; Bacteria.
DR HOGENOM; CLU_033732_3_0_9; -.
DR OMA; LMMDIRH; -.
DR Proteomes; UP000000269; 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 InterPro; IPR005225; Small_GTP-bd_dom.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03598; GTPase_YsxC; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 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..208
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_1000059467"
FT DOMAIN 22..195
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 174..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
SQ SEQUENCE 208 AA; 23668 MW; 3D0BBD2AC2860238 CRC64;
MKVISSEIVI SAVAPKQYPE NGLPEIALAG RSNVGKSSTV NTILKRRKLA RVSASPGKTR
TINFYIVNNE FHIVDLPGYG YAKVSKGEKE TWGKMMETYL SSRKNLYEVI LLVDIRHEPT
ADDKMMYDWI KHYGYGSIVI ATKSDKISRG AYQKHFKMIR EKLGMSPEDK IIPISSLKRE
GIDKLWHSIE EIFIANNLPI TIEEAEEY