ID A0A1Y4S4C2_9FIRM Unreviewed; 199 AA.
AC A0A1Y4S4C2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000256|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000256|HAMAP-Rule:MF_00321,
GN ECO:0000313|EMBL:OUQ24704.1};
GN ORFNames=B5E80_06275 {ECO:0000313|EMBL:OUQ24704.1};
OS Flavonifractor sp. An135.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Flavonifractor.
OX NCBI_TaxID=1965558 {ECO:0000313|EMBL:OUQ24704.1, ECO:0000313|Proteomes:UP000196472};
RN [1] {ECO:0000313|Proteomes:UP000196472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An135 {ECO:0000313|Proteomes:UP000196472};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUQ24704.1}.
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DR EMBL; NFLG01000008; OUQ24704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4S4C2; -.
DR OrthoDB; 9804921at2; -.
DR Proteomes; UP000196472; 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 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:UP000196472};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00321}.
FT DOMAIN 24..197
FT /note="EngB-type G"
FT /evidence="ECO:0000259|PROSITE:PS51706"
SQ SEQUENCE 199 AA; 22123 MW; 82635D9FE465B152 CRC64;
MPLNLNNAEF VRSAAKAADF PRDALPQIVF AGRSNVGKSS VINRLLGRKN FARVGNSPGK
TTHINYFLID KKLYLVDLPG YGYAKVSQAE KARWGRLIES WFADPALMTL GVLIVDARHK
PTADDCTMAE WFQNSGKPFA VVANKLDKLK KSEIEPNLER IRETLSLDED TPLIPFSAEK
GNGRDVLLAL VEAHREGMQ
//