ID A0A223CZX2_9BACL Unreviewed; 203 AA.
AC A0A223CZX2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CIG75_07855 {ECO:0000313|EMBL:ASS74902.1};
OS Tumebacillus algifaecis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS74902.1, ECO:0000313|Proteomes:UP000214688};
RN [1] {ECO:0000313|EMBL:ASS74902.1, ECO:0000313|Proteomes:UP000214688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=THMBR28 {ECO:0000313|EMBL:ASS74902.1,
RC ECO:0000313|Proteomes:UP000214688};
RX PubMed=25858243; DOI=10.1099/ijs.0.000240;
RA Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.;
RT "Tumebacillus algifaecis sp. nov., isolated from decomposing algal scum.";
RL Int. J. Syst. Evol. Microbiol. 65:2194-2198(2015).
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; CP022657; ASS74902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223CZX2; -.
DR KEGG; tab:CIG75_07855; -.
DR OrthoDB; 9804921at2; -.
DR Proteomes; UP000214688; 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}; Reference proteome {ECO:0000313|Proteomes:UP000214688};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00321}.
FT DOMAIN 22..195
FT /note="EngB-type G"
FT /evidence="ECO:0000259|PROSITE:PS51706"
SQ SEQUENCE 203 AA; 22768 MW; 1EAF77EA004CE852 CRC64;
MMIREAKFII SAVKPHQYPE GDLPEIALAG RSNVGKSSLI NRLLHRRGLA RTSGTPGKTQ
QLNYYLLNED MYLVDLPGYG FAKVPKDVKA QWGKMIGTYL DQRENLKLVM QLIDIRHAPS
KEDVEMYQYL AHYARPHAII VTKADKVARG QYQKHIKVIR ETLNVLPGTP IILTSADSGL
GKQEVWDLVA KHIGVEEIIA PSG
//
