CAZyme Information: MGYG000000135_02935

Basic Information

• Species: Murimonas intestini
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Murimonas; Murimonas intestini
• CAZyme ID: MGYG000000135_02935
• CAZy Family: GT51
• CAZyme Description: Penicillin-binding protein 1F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
225	MGYG000000135_6|CGC1	25304.86	4.8303

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000135	5745007	Isolate	Canada	North America

• Gene Location: Start: 107644; End: 108321 Strand: -

Full Sequence      

MRILKAVGKIAAVLFLICICVCGYFAYQGYQMYHKAEAAQSLEAKVDEIRSQPGYTSIKD
MPLTYLEAVVAVEDHRFYDHFGIDIIAIGRAVVNNVKALSFVEGGSTITQQLAKNLYFTQ
EKEMTRKAAEVFAAFDLERHYTKDEILELYVNTIYFGSGYYGVGEASEGYFGKEPRYLTD
DECTMLAGIPNAPSVYDPRVNPELAKERQQQVVNQMIENGFVPAQ

Enzyme Prediction     

No EC number prediction in MGYG000000135_02935.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	52	216	6.9e-64	0.9265536723163842

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	2.34e-83	55	216	15	176	Transglycosylase. The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
TIGR02074	PBP_1a_fam	9.75e-82	55	225	4	174	penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
COG5009	MrcA	5.04e-71	1	225	2	239	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG0744	MrcB	1.03e-69	55	225	78	249	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	6.29e-45	42	222	57	235	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRP41835.1	6.23e-86	1	221	1	221
ASN93505.1	6.23e-86	1	221	1	221
ASB42272.1	1.48e-85	2	218	9	225
ANU54501.1	1.48e-85	2	218	9	225
QQR31552.1	1.48e-85	2	218	9	225

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	2.32e-48	55	222	22	189	Crystalstructure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis [Aquifex aeolicus VF5],3D3H_A Crystal structure of a complex of the peptidoglycan glycosyltransferase domain from Aquifex aeolicus and neryl moenomycin A [Aquifex aeolicus],3NB7_A Crystal structure of Aquifex Aeolicus Peptidoglycan Glycosyltransferase in complex with Decarboxylated Neryl Moenomycin [Aquifex aeolicus]
3NB6_A	9.29e-48	55	222	22	189	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
4OON_A	7.90e-40	42	225	30	211	Crystalstructure of PBP1a in complex with compound 17 ((4Z,8S,11E,14S)-5-(2-amino-1,3-thiazol-4-yl)-14-(5,6-dihydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-8-formyl-2-methyl-6-oxo-3,10-dioxa-4,7,11-triazatetradeca-4,11-diene-2,12,14-tricarboxylic acid) [Pseudomonas aeruginosa PAO1]
3UDF_A	1.23e-36	59	222	45	208	ChainA, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDF_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii]
5U2G_A	3.15e-35	42	222	31	209	2.6Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20],5U2G_B 2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38050	4.22e-47	57	224	71	238	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O87626	1.84e-46	55	225	70	240	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
O87579	1.69e-45	55	225	70	240	Penicillin-binding protein 1A OS=Neisseria lactamica OX=486 GN=mrcA PE=3 SV=1
O86088	3.18e-45	55	225	70	240	Penicillin-binding protein 1A OS=Neisseria cinerea OX=483 GN=mrcA PE=3 SV=1
Q07259	3.99e-45	41	222	36	215	Putative transglycosylase H16_A0665 OS=Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) OX=381666 GN=H16_A0665 PE=3 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
0.879715	0.012831	0.100707	0.000101	0.000053	0.006611

TMHMM  Annotations     

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