CAZyme Information: MGYG000000425_01317

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae
• CAZyme ID: MGYG000000425_01317
• CAZy Family: GT51
• CAZyme Description: Penicillin-binding protein 1A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
203	MGYG000000425_41|CGC1	23287.01	9.3485

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000425	1738291	MAG	Sweden	Europe

• Gene Location: Start: 10029; End: 10640 Strand: -

Full Sequence      

MKKFIKRFTVIVLFSAVAVCVVCGPMIKSGYEMYKQAVLRQPIEEKVRQIRQSRRYTDFD
EISPEFIERLLASEDRRFYYHRAIDPIALARAVVVNITKGKYEQGGSTITQQLAKNMYFS
FEKKVERKIAEVFVASKLEDEYSKNDILALYCAMAYFGENCYGVKQASLHYYGVEPARLN
REQAAELVATLKAPSVFNPSTMG

Enzyme Prediction     

No EC number prediction in MGYG000000425_01317.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	49	201	5.7e-55	0.864406779661017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	9.40e-67	51	201	10	160	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.
COG0744	MrcB	1.43e-59	47	199	69	222	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
TIGR02074	PBP_1a_fam	8.75e-55	54	199	2	147	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	3.78e-49	1	199	1	212	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG4953	PbpC	3.62e-39	54	199	58	202	Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABX41988.1	2.46e-68	2	200	3	201
SET84136.1	7.81e-65	24	200	26	202
BBF43413.1	7.35e-60	1	199	1	199
QQY26839.1	4.74e-57	1	202	1	199
QQV06180.1	4.74e-57	1	202	1	199

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NB6_A	2.40e-36	52	199	18	165	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A	3.39e-36	52	199	18	165	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	4.75e-28	58	199	43	184	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	1.26e-25	61	199	47	185	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]
3VMA_A	1.06e-24	67	199	190	326	CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O66874	1.48e-32	52	199	61	208	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
Q9KNU5	4.90e-29	3	199	2	211	Penicillin-binding protein 1A OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=mrcA PE=3 SV=2
P02918	6.71e-29	60	199	72	211	Penicillin-binding protein 1A OS=Escherichia coli (strain K12) OX=83333 GN=mrcA PE=1 SV=1
P39793	9.26e-29	52	199	93	241	Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 SV=1
P38050	1.39e-27	52	199	65	212	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.054631	0.001342	0.944004	0.000005	0.000007	0.000031

TMHMM  Annotations     

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