ENGB_ECOLI
ID ENGB_ECOLI Reviewed; 210 AA.
AC P0A6P7; P24253; P76771; Q2M8G2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; Synonyms=yihA;
GN OrderedLocusNames=b3865, JW5930;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6183253; DOI=10.1128/jb.152.3.1211-1219.1982;
RA Joyce C.M., Grindley N.D.;
RT "Identification of two genes immediately downstream from the polA gene of
RT Escherichia coli.";
RL J. Bacteriol. 152:1211-1219(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=10572302; DOI=10.1016/s0300-9084(99)00207-2;
RA Dassain M., Leroy A., Colosetti L., Carole S., Bouche J.-P.;
RT "A new essential gene of the 'minimal genome' affecting cell division.";
RL Biochimie 81:889-895(1999).
RN [6]
RP IDENTIFICATION OF START CODON.
RA Loferer H.;
RL Submitted (MAR-1998) to UniProtKB.
CC -!- FUNCTION: Necessary for normal cell division and for the maintenance of
CC normal septation. Depletion of this protein leads to a severe reduction
CC in growth rate and to extensive filamentation, with a block beyond the
CC stage of segregation. Essential for bacteria survival.
CC {ECO:0000255|HAMAP-Rule:MF_00321, ECO:0000269|PubMed:10572302}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00321};
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngB GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00321}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB02999.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE77444.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J01663; AAA24403.1; ALT_INIT; Genomic_DNA.
DR EMBL; L19201; AAB02999.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76862.3; -; Genomic_DNA.
DR EMBL; AP009048; BAE77444.1; ALT_INIT; Genomic_DNA.
DR PIR; S40810; S40810.
DR RefSeq; NP_418301.3; NC_000913.3.
DR RefSeq; WP_000183349.1; NZ_STEB01000017.1.
DR PDB; 1PUI; X-ray; 2.00 A; A/B=1-210.
DR PDBsum; 1PUI; -.
DR AlphaFoldDB; P0A6P7; -.
DR SMR; P0A6P7; -.
DR BioGRID; 4262625; 413.
DR DIP; DIP-48178N; -.
DR STRING; 511145.b3865; -.
DR jPOST; P0A6P7; -.
DR PaxDb; P0A6P7; -.
DR PRIDE; P0A6P7; -.
DR EnsemblBacteria; AAC76862; AAC76862; b3865.
DR EnsemblBacteria; BAE77444; BAE77444; BAE77444.
DR GeneID; 66672230; -.
DR GeneID; 948358; -.
DR KEGG; ecj:JW5930; -.
DR KEGG; eco:b3865; -.
DR PATRIC; fig|1411691.4.peg.2848; -.
DR EchoBASE; EB1188; -.
DR eggNOG; COG0218; Bacteria.
DR HOGENOM; CLU_033732_1_0_6; -.
DR InParanoid; P0A6P7; -.
DR OMA; LMMDIRH; -.
DR PhylomeDB; P0A6P7; -.
DR BioCyc; EcoCyc:EG11203-MON; -.
DR EvolutionaryTrace; P0A6P7; -.
DR PRO; PR:P0A6P7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IDA:EcoCyc.
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; -; 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 Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03598; GTPase_YsxC; 1.
DR PROSITE; PS51706; G_ENGB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..210
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_0000157747"
FT DOMAIN 25..199
FT /note="EngB-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 78..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 145..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 178..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1PUI"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1PUI"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1PUI"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:1PUI"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1PUI"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:1PUI"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1PUI"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:1PUI"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:1PUI"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:1PUI"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1PUI"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1PUI"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:1PUI"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1PUI"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1PUI"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:1PUI"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:1PUI"
SQ SEQUENCE 210 AA; 23561 MW; 11BCA2ED59220C0D CRC64;
MTNLNYQQTH FVMSAPDIRH LPSDTGIEVA FAGRSNAGKS SALNTLTNQK SLARTSKTPG
RTQLINLFEV ADGKRLVDLP GYGYAEVPEE MKRKWQRALG EYLEKRQSLQ GLVVLMDIRH
PLKDLDQQMI EWAVDSNIAV LVLLTKADKL ASGARKAQLN MVREAVLAFN GDVQVETFSS
LKKQGVDKLR QKLDTWFSEM QPVEETQDGE
