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Database: UniProt
Entry: A0A1W1VEM4_PEPAS
LinkDB: A0A1W1VEM4_PEPAS
Original site: A0A1W1VEM4_PEPAS 
ID   A0A1W1VEM4_PEPAS        Unreviewed;       203 AA.
AC   A0A1W1VEM4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Probable GTP-binding protein EngB {ECO:0000256|HAMAP-Rule:MF_00321};
GN   Name=engB {ECO:0000256|HAMAP-Rule:MF_00321};
GN   ORFNames=SAMN00017477_1853 {ECO:0000313|EMBL:SMB91822.1};
OS   Peptoniphilus asaccharolyticus DSM 20463.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=573058 {ECO:0000313|EMBL:SMB91822.1, ECO:0000313|Proteomes:UP000192368};
RN   [1] {ECO:0000313|EMBL:SMB91822.1, ECO:0000313|Proteomes:UP000192368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20463 {ECO:0000313|EMBL:SMB91822.1,
RC   ECO:0000313|Proteomes:UP000192368};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FWWR01000013; SMB91822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1VEM4; -.
DR   STRING; 573058.SAMN00017477_1853; -.
DR   OrthoDB; 9804921at2; -.
DR   Proteomes; UP000192368; Unassembled WGS sequence.
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   203 AA;  23117 MW;  F5922D29107D46FB CRC64;
     MKTDDARLEQ VAVKKEQYPE ADVYEFAFAG RSNVGKSSFI NAMLGRKNLA RTSSAPGKTR
     TINFYRVSDL RLVDLPGYGY ARVSKIERNS WAGVINTYLE NRENLLEVLL LVDIRHEPSE
     LDKAMYDYLI ANGHSGLVIA TKADKISRGQ YQNHIAKIQK KLGIKNRDNI IPFSSVDKKM
     VDEMWDIFED IVGFYDGSEE DEL
//
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