CAZyme Information: MGYG000002512_02864

Basic Information

• Species: Morganella morganii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Morganella; Morganella morganii
• CAZyme ID: MGYG000002512_02864
• CAZy Family: GT4
• CAZyme Description: Glutamate/aspartate import solute-binding protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
298	MGYG000002512_1|CGC27	32702.19	7.8581

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002512	3906921	Isolate	not provided	not provided

• Gene Location: Start: 2912142; End: 2913038 Strand: +

Full Sequence      

MRKLVLSVLVTGAALASAAVSAEELAGTLKKINDSGVIVVGHRESSVPFSYYDNQQNVVG
YSQDYSNHIVDAVKKTLNKPDLQVKLIPVTSQNRIPLLQNGTFDFECGSTTNNLARQQQA
AFSNTIFVVGTRLLTGKDSGIKDFADLAGKNVVVTSGTTSEMLLNKLNDEKQMKMRIISA
KDHGDAFRTLESGRAVAFMMDDALLAGERAKAKKPDNWVIVGTPQSEEAYGCMLRKDDPQ
FKALIDKTVSDAQTSGEAEKSYTRWFKQPIPPKNLNLNFELSDEMKGLFKAPNDKAFE

Enzyme Prediction     

No EC number prediction in MGYG000002512_02864.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10797	PRK10797	0.0	1	296	3	300	glutamate and aspartate transporter subunit; Provisional
cd13688	PBP2_GltI_DEBP	1.31e-113	29	266	1	238	Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic binding protein fold. This subfamily represents the periplasmic-binding protein component of ABC transporter specific for carboxylic amino acids, including GtlI from Escherichia coli. The aspartate-glutamate binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
cd01000	PBP2_Cys_DEBP_like	3.97e-82	29	266	1	228	Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold. This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
cd13689	PBP2_BsGlnH	7.83e-64	29	267	1	229	Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 periplasmic-bindig protein fold. This group includes periplasmic glutamine-binding domain GlnP from Bacillus subtilis and its related proteins. The GlnP domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
smart00062	PBPb	5.40e-56	37	266	1	219	Bacterial periplasmic substrate-binding proteins. bacterial proteins, eukaryotic ones are in PBPe

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QET99138.1	8.20e-178	1	296	3	295
BBV07546.1	8.20e-178	1	296	3	295
QIB31157.1	8.20e-178	1	296	3	295
QUC26646.1	8.20e-178	1	296	3	295
AXO20211.1	8.20e-178	1	296	3	295

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHA_A	3.54e-164	28	296	9	277	DEBP[Shigella flexneri],2VHA_B DEBP [Shigella flexneri]
2IA4_A	6.18e-158	28	296	9	277	Crystalstructure of Novel amino acid binding protein from Shigella flexneri [Shigella flexneri 2a str. 301],2IA4_B Crystal structure of Novel amino acid binding protein from Shigella flexneri [Shigella flexneri 2a str. 301]
5EYF_A	1.30e-21	29	266	8	236	CrystalStructure of Solute-binding Protein from Enterococcus faecium with Bound Glutamate [Enterococcus faecium DO],5EYF_B Crystal Structure of Solute-binding Protein from Enterococcus faecium with Bound Glutamate [Enterococcus faecium DO]
6MLO_E	7.43e-14	40	266	8	231	Crystalstructure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) Y14A mutant from Salmonella typhimurium complexed with arginine [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],6MLP_E Crystal structure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) Y14A mutant from Salmonella typhimurium complexed with histidine [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],6MLV_A Crystal structure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) Y14A mutant from Salmonella typhimurium [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
6MKW_A	1.37e-13	40	266	7	230	Crystalstructure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) D11A mutant from Salmonella typhimurium complexed with histidine [Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZF60	2.86e-164	1	296	3	300	Glutamate/aspartate import solute-binding protein OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=gltI PE=3 SV=3
P37902	2.73e-162	9	296	13	300	Glutamate/aspartate import solute-binding protein OS=Escherichia coli (strain K12) OX=83333 GN=gltI PE=1 SV=2
Q9I402	1.80e-120	13	298	14	300	L-glutamate/L-aspartate-binding protein OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=PA1342 PE=1 SV=1
O34563	8.72e-22	21	268	31	269	ABC transporter glutamine-binding protein GlnH OS=Bacillus subtilis (strain 168) OX=224308 GN=glnH PE=2 SV=1
P27676	6.60e-19	21	248	42	262	Glutamine-binding protein OS=Geobacillus stearothermophilus OX=1422 GN=glnH PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000321	0.999009	0.000167	0.000179	0.000172	0.000150

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002512_02864.