ID D3P9A8_DEFDS Unreviewed; 191 AA.
AC D3P9A8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000256|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000256|HAMAP-Rule:MF_00321};
GN OrderedLocusNames=DEFDS_1843 {ECO:0000313|EMBL:BAI81298.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI81298.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI81298.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(2010).
CC -!- FUNCTION: Necessary for normal cell division and for the maintenance of
CC normal septation. {ECO:0000256|HAMAP-Rule:MF_00321}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngB GTPase family. {ECO:0000256|ARBA:ARBA00009638,
CC ECO:0000256|HAMAP-Rule:MF_00321}.
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DR EMBL; AP011529; BAI81298.1; -; Genomic_DNA.
DR RefSeq; WP_013008543.1; NC_013939.1.
DR AlphaFoldDB; D3P9A8; -.
DR STRING; 639282.DEFDS_1843; -.
DR KEGG; ddf:DEFDS_1843; -.
DR eggNOG; COG0218; Bacteria.
DR HOGENOM; CLU_033732_3_0_0; -.
DR OrthoDB; 9804921at2; -.
DR Proteomes; UP000001520; 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 InterPro; IPR005225; Small_GTP-bd_dom.
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 {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00321};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00321};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00321}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00321}; Reference proteome {ECO:0000313|Proteomes:UP000001520};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00321}.
FT DOMAIN 19..191
FT /note="EngB-type G"
FT /evidence="ECO:0000259|PROSITE:PS51706"
SQ SEQUENCE 191 AA; 21903 MW; 7A37276C65D4EBC2 CRC64;
MKAEYIKSAV YEKDYPDTDL PEIAFVGRSN VGKSSMINTL VNRKKLVKVS QKPGKTRTIN
FFNINDELIF VDLPGYGYAK VSKKDRELWK VMIETYLTKR SQLKAVVLII DIRVGPTNDD
KLMYEWFMAY NVPTIVAFTK CDKLSNNKIQ KQLAIIKKEF GDGLGDYVLF SSVTRRGKDE
LWGIIKEKAS L
//
