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Database: UniProt
Entry: E8T4A4_THEA1
LinkDB: E8T4A4_THEA1
Original site: E8T4A4_THEA1 
ID   E8T4A4_THEA1            Unreviewed;       194 AA.
AC   E8T4A4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=Theam_1472 {ECO:0000313|EMBL:ADU97433.1};
OS   Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1).
OC   Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC   Desulfurobacteriaceae; Thermovibrio.
OX   NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU97433.1, ECO:0000313|Proteomes:UP000006362};
RN   [1] {ECO:0000313|EMBL:ADU97433.1, ECO:0000313|Proteomes:UP000006362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15698 / JCM 12110 / HB-1
RC   {ECO:0000313|Proteomes:UP000006362};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C., Woyke T.;
RT   "Complete sequence of chromosome of Thermovibrio ammonificans HB-1.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002444; ADU97433.1; -; Genomic_DNA.
DR   RefSeq; WP_013538219.1; NC_014926.1.
DR   AlphaFoldDB; E8T4A4; -.
DR   STRING; 648996.Theam_1472; -.
DR   KEGG; tam:Theam_1472; -.
DR   eggNOG; COG0218; Bacteria.
DR   HOGENOM; CLU_033732_3_0_0; -.
DR   OrthoDB; 9804921at2; -.
DR   Proteomes; UP000006362; 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 {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};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00321}.
FT   DOMAIN          22..194
FT                   /note="EngB-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51706"
SQ   SEQUENCE   194 AA;  22315 MW;  E673463BD79D6D31 CRC64;
     MKVKKVQLYK TVYTPDELPQ TPYNEVAFVG RSNVGKSSLL NAVANNFKLA KVSSQPGKTR
     SINFYLVNDR FFLVDLPGYG FAKVPLKEQQ RWRELIESYL KGRDRLKGVF LLVDSKVGPT
     EKDLQMKEWL DFFGIPYTVV ATKVDRLKAS QRRNLEERIK KALGGGDFKV IPFSAKTREG
     REVLLREIFN YIES
//
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