CAZyme Information: MGYG000001255_02099

Basic Information

• Species: Faecalibacterium prausnitzii_F
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium prausnitzii_F
• CAZyme ID: MGYG000001255_02099
• CAZy Family: GT51
• CAZyme Description: Penicillin-binding protein 1A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
245	MGYG000001255_37|CGC1	27221.36	7.2606

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001255	2423712	MAG	Austria	Europe

• Gene Location: Start: 15415; End: 16152 Strand: -

Full Sequence      

MFHRFFCFLKRSLLTVLLVLLLLLLAAGGWFVYQGRQLYQSAASVTPIATLYDTISSRTH
YAAYDQLPQTFVQAVICTEDEHFMTHKGIDPGAIFRALLYDLRTRSLAEGGSTLTQQLAK
NALFTQEKRLTRKAAEAFAAIDMEKAYSKQQIFEMYANTIYFGNGCYGIEEAAEGYFGKT
AAELTDAEAVYLAGLPNAPSAYASNPELALKRAQVVLKRMVKCRVFTQQQADEVAAEVAA
LPILQ

Enzyme Prediction     

No EC number prediction in MGYG000001255_02099.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	55	221	2.1e-61	0.9491525423728814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	3.40e-79	46	221	3	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	1.40e-69	61	230	4	175	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	1.96e-68	47	230	65	250	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	1.46e-61	55	230	63	240	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	7.87e-45	65	230	72	239	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATL90873.1	2.46e-84	8	243	5	240
ATP00668.1	2.46e-84	8	243	5	240
QIA43609.1	2.46e-84	8	243	5	240
SET89048.1	2.11e-59	33	241	27	237
QNM09777.1	3.59e-59	31	238	35	244

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NB6_A	8.93e-48	47	233	7	196	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A	3.57e-47	47	233	7	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]
4OON_A	6.67e-34	64	237	44	218	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]
5U2G_A	9.34e-34	67	237	48	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]
3UDF_A	1.39e-30	64	237	44	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O66874	3.42e-42	30	233	39	239	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
P02918	2.75e-35	65	237	72	246	Penicillin-binding protein 1A OS=Escherichia coli (strain K12) OX=83333 GN=mrcA PE=1 SV=1
P70997	7.31e-35	70	237	85	254	Penicillin-binding protein 2D OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpG PE=2 SV=3
Q9KNU5	1.26e-34	65	237	72	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
P39793	1.79e-34	61	222	97	261	Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 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
0.977497	0.002330	0.003644	0.000026	0.000012	0.016500

TMHMM  Annotations     

start	end
12	34