CAZyme Information: MGYG000002264_01533

Basic Information

• Species: UMGS363 sp900550695
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UMGS363; UMGS363 sp900550695
• CAZyme ID: MGYG000002264_01533
• CAZy Family: GT51
• CAZyme Description: Penicillin-binding protein 1A/1B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
237		26256.28	4.9115

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002264	2273272	MAG	Peru	South America

• Gene Location: Start: 3266; End: 3979 Strand: +

Full Sequence      

MFKRLLNILMNLIILAAVIMLILLGVVGVRGFMLYKTRTDYRSLSAVAGEIRSEPLFTPT
EELPDFYLKAVVAIEDRDFYRHSGIKVTSMLRALIADVKAGAPVQGGSTITQQLAKNELF
TQEKTVDRKAAEIFAAFTLEREFTKNEILELYVNSIYFGDGYHGIGAAAEGLFGKNPSEL
TRFECAELAGIPNAPAKYSVRFAPDEVEKRGEEVLKAMLSAGSITESEYDEILAEKN

Enzyme Prediction     

No EC number prediction in MGYG000002264_01533.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	57	218	1.9e-57	0.9096045197740112

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	4.22e-72	58	219	16	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	7.94e-68	57	231	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	6.51e-66	1	236	7	258	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	2.82e-62	9	235	1	247	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	1.22e-47	12	236	7	247	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAK43832.1	4.49e-72	28	224	39	235
QOS67703.1	3.76e-71	15	233	23	242
ACV56467.1	5.65e-68	15	220	23	229
APO31194.1	5.65e-68	15	220	23	229
CBL03605.1	9.84e-66	30	235	39	244

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	3.90e-47	57	231	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]
3NB6_A	1.56e-46	57	231	22	196	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
4OON_A	1.75e-35	36	235	22	219	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	1.68e-33	61	235	45	219	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	2.51e-33	49	235	36	220	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
O66874	1.92e-42	57	231	65	239	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
Q07259	4.51e-38	16	235	6	226	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
P38050	1.59e-37	62	228	74	240	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
P39793	1.60e-37	42	230	85	271	Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 SV=1
Q9KNU5	7.02e-37	44	235	57	246	Penicillin-binding protein 1A OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=mrcA 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
0.993612	0.001729	0.000378	0.000013	0.000008	0.004299

TMHMM  Annotations     

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