UniProt Accession

 ENGB_ECOLI; P0A6P7; P24253; P76771; Q2M8G2 

Genbank Protein ID

 J01663; L19201; U00096; AP009048 

Genbank Nucleotide ID

 AAA24403.1; AAB02999.1; AAC76862.3; BAE77444.1 

Protein Name

 Probable GTP-binding protein EngB 

Protein Synonyms/Alias

  

Gene Name

 engB 

Gene Synonyms/Alias

 yihA; b3865; JW5930 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
50	LNTLTNQKSLARTSK	acetylation	[1]
74	LFEVADGKRLVDLPG	acetylation	[1]
92	AEVPEEMKRKWQRAL	acetylation	[1]
105	ALGEYLEKRQSLQGL	acetylation	[1]
149	VLLTKADKLASGARK	acetylation	[1, 2]
183	ETFSSLKKQGVDKLR	acetylation	[1]
188	LKKQGVDKLRQKLDT	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 Necessary for normal cell division and for the maintenance of normal septation. Depletion of this protein leads to a severe reduction in growth rate and to extensive filamentation, with a block beyond the stage of segregation. Essential for bacteria survival. 

Sequence Annotation

 DOMAIN 38 146 G.
 NP_BIND 33 40 GTP (Potential).
 NP_BIND 78 82 GTP (Potential).
 NP_BIND 145 148 GTP (Potential).  

Keyword

 3D-structure; Cell cycle; Cell division; Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome; Septation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 210 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0000917; P:barrier septum assembly; IEA:HAMAP.
 GO:0000910; P:cytokinesis; IMP:EcoCyc. 

Interpro

 IPR019987; GTP-bd_ribosome_bio_YsxC.
 IPR006073; GTP_binding_domain.
 IPR027417; P-loop_NTPase. 

Pfam

 PF01926; MMR_HSR1 

SMART

  

PROSITE

  

PRINTS