CAZyme Information: MGYG000002344_01164

Basic Information

• Species: Acinetobacter baumannii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter baumannii
• CAZyme ID: MGYG000002344_01164
• CAZy Family: CBM50
• CAZyme Description: putative protein YgaU

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
157		16888.23	4.7688

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002344	3953404	Isolate	United States	North America

• Gene Location: Start: 1195426; End: 1195899 Strand: -

Full Sequence      

MGLFDFVKGIGKKNTAPAEPQAAPATPAEPSAQEIANKLLGLIKSLGLGVEGLSVTYNGS
TDTAIIKGQVQSQADKEKIILIVGNVDHVAQVDDQMTVATPEPESKFYTVKSGDNLSKIA
KEFYGDANQYQKIFEANKPMLKDPDEIFPGQVLRIPQ

Enzyme Prediction     

No EC number prediction in MGYG000002344_01164.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK11198	PRK11198	5.55e-74	1	157	1	147	LysM domain/BON superfamily protein; Provisional
COG1652	XkdP	6.74e-16	105	157	210	263	Nucleoid-associated protein YgaU, contains BON and LysM domains [Function unknown].
cd00118	LysM	1.03e-11	106	155	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
smart00257	LysM	1.46e-09	107	155	1	44	Lysin motif.
pfam01476	LysM	8.59e-09	108	156	1	43	LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ARG29438.1	3.15e-108	1	157	1	157
ADX91245.1	3.15e-108	1	157	1	157
AHJ92266.1	3.15e-108	1	157	1	157
AUT39780.1	3.15e-108	1	157	1	157
SBS23202.1	3.15e-108	1	157	1	157

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FIM_A	3.74e-38	1	157	1	148	Thestructure of Kbp.K from E. coli [Escherichia coli],7PVC_A Chain A, Potassium binding protein Kbp [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0ADE6	1.62e-37	1	157	1	148	Potassium binding protein Kbp OS=Escherichia coli (strain K12) OX=83333 GN=kbp PE=1 SV=2
P0ADE7	1.62e-37	1	157	1	148	Potassium binding protein Kbp OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=kbp PE=3 SV=2
Q9RVY3	1.92e-09	35	156	123	252	Uncharacterized protein DR_0888 OS=Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) OX=243230 GN=DR_0888 PE=1 SV=1
P54335	2.43e-07	106	157	159	219	Phage-like element PBSX protein XkdP OS=Bacillus subtilis (strain 168) OX=224308 GN=xkdP PE=4 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000012	0.000034	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002344_01164.