CAZyme Information: MGYG000000132_02205

Basic Information

• Species: Beduini sp902363625
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Beduini; Beduini sp902363625
• CAZyme ID: MGYG000000132_02205
• CAZy Family: GT51
• CAZyme Description: Penicillin-binding protein 1F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
240	MGYG000000132_7|CGC1	27309.28	4.4998

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000132	2897757	Isolate	Canada	North America

• Gene Location: Start: 216168; End: 216890 Strand: +

Full Sequence      

MKYIKRLLMLLIVIVLVIGGYYVYLGYQMYDKAKEEKPFDEMVETIKSNQSYTSLDQLPS
IYLDAVIAVEDHRFYEHGGIDVLAIGRAIGNDIISLSFKEGGSTITQQLAKNLYFTQEKK
IERKIAEVFMAFDIEKTCSKDEILELYLNTIYFGDGYYCVKDASLGYFDKLPSEMNEYEA
TLLAGIPNAPSAYSPTNSTVLASQRQRQVLERMVKCNYLDQEEADKIAALGSVEQIDRID

Enzyme Prediction     

No EC number prediction in MGYG000000132_02205.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	43	214	1e-60	0.9661016949152542

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	6.42e-79	49	214	12	177	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	1.04e-73	52	226	4	178	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]
COG0744	MrcB	1.95e-67	52	226	78	253	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	2.67e-65	42	226	59	243	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	6.26e-47	54	226	70	242	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJU22158.1	2.49e-89	26	232	29	235
QRP41835.1	2.87e-88	26	232	29	235
ASN93505.1	2.87e-88	26	232	29	235
ANU46909.1	1.91e-86	26	232	29	235
QQQ98385.1	1.91e-86	26	232	29	235

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NB6_A	1.55e-41	52	226	22	196	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A	2.19e-41	52	226	22	196	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]
3UDF_A	1.74e-35	57	229	46	218	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	2.34e-34	33	225	3	215	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]
4OON_A	3.10e-34	58	222	47	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38050	8.97e-41	23	224	31	241	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
Q07259	3.16e-39	33	225	30	221	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
O87626	1.79e-38	47	226	65	244	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
O87579	2.45e-38	47	226	65	244	Penicillin-binding protein 1A OS=Neisseria lactamica OX=486 GN=mrcA PE=3 SV=1
P0A0Z5	6.22e-38	47	226	65	244	Penicillin-binding protein 1A OS=Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) OX=122587 GN=mrcA PE=3 SV=1

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
0.992059	0.004489	0.002524	0.000032	0.000016	0.000910

TMHMM  Annotations     

start	end
7	29