dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003797_00283

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Basic Information help

Species

Lineage

Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus;

CAZyme ID

MGYG000003797_00283

CAZy Family

GT51

CAZyme Description

Penicillin-binding protein 1A/1B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
531	MGYG000003797_14\|CGC1	58018.86	8.9244

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003797	1673820	MAG	Canada	North America

Gene Location

Start: 158; End: 1753 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003797_00283.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT51	112	302	5.1e-52	0.9887005649717514

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0744	MrcB	1.07e-114	54	526	11	431	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
pfam00912	Transgly	1.13e-52	112	303	1	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.
COG4953	PbpC	5.55e-46	131	521	64	396	Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	2.45e-40	53	521	4	523	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	5.13e-24	111	408	53	305	penicillin-binding protein 1a; Provisional

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
BAD00804.1	1	527	1	527
BAD00790.1	1	527	1	527
BAD00816.1	1	527	1	527
AJD73060.1	1	527	1	527
VFI25897.1	1	527	1	527

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2JE5_A	1.74e-309	73	527	2	456	StructuralAnd Mechanistic Basis Of Penicillin Binding Protein Inhibition By Lactivicins [Streptococcus pneumoniae R6],2JE5_B Structural And Mechanistic Basis Of Penicillin Binding Protein Inhibition By Lactivicins [Streptococcus pneumoniae R6]
2Y2G_A	1.42e-135	321	527	24	230	Penicillin-BindingProtein 1b (Pbp-1b) In Complex With An Alkyl Boronate (A01) [Streptococcus pneumoniae R6],2Y2G_B Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (A01) [Streptococcus pneumoniae R6],2Y2H_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za2) [Streptococcus pneumoniae R6],2Y2H_B Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za2) [Streptococcus pneumoniae R6],2Y2I_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za3) [Streptococcus pneumoniae R6],2Y2J_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za4) [Streptococcus pneumoniae R6],2Y2K_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za5) [Streptococcus pneumoniae R6],2Y2L_A Penicillin-binding Protein 1b (pbp-1b) In Complex With An Alkyl Boronate (e06) [Streptococcus pneumoniae R6],2Y2L_B Penicillin-binding Protein 1b (pbp-1b) In Complex With An Alkyl Boronate (e06) [Streptococcus pneumoniae R6],2Y2M_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (E08) [Streptococcus pneumoniae R6],2Y2N_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (E07) [Streptococcus pneumoniae R6],2Y2O_A Penicillin-binding Protein 1b (pbp-1b) In Complex With An Alkyl Boronate (eo9) [Streptococcus pneumoniae R6],2Y2P_A Penicillin-binding protein 1b (pbp-1b) in complex with an alkyl boronate (z10) [Streptococcus pneumoniae R6],2Y2Q_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Z06) [Streptococcus pneumoniae R6],2Y2Q_B Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Z06) [Streptococcus pneumoniae R6]
2BG1_A	5.67e-135	321	527	24	230	Activesite restructuring regulates ligand recognition in classA Penicillin-binding proteins (PBPs) [Streptococcus pneumoniae R6],2XD5_A Structural insights into the catalytic mechanism and the role of Streptococcus pneumoniae PBP1b [Streptococcus pneumoniae R6],2XD5_B Structural insights into the catalytic mechanism and the role of Streptococcus pneumoniae PBP1b [Streptococcus pneumoniae R6]
2XD1_A	5.67e-135	321	527	24	230	ACTIVESITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASS A PENICILLIN-BINDING PROTEINS [Streptococcus pneumoniae R6],2XD1_B ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASS A PENICILLIN-BINDING PROTEINS [Streptococcus pneumoniae R6]
2UWX_A	3.21e-134	321	527	24	230	Activesite restructuring regulates ligand recognition in class A penicillin-binding proteins [Streptococcus pneumoniae R6]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0TNZ8	7.81e-43	99	521	62	484	Penicillin-binding protein 1A OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=pbpA PE=3 SV=1
Q8XJ01	1.04e-42	99	521	62	484	Penicillin-binding protein 1A OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=pbpA PE=3 SV=1
Q0SRL7	5.19e-41	99	521	62	484	Penicillin-binding protein 1A OS=Clostridium perfringens (strain SM101 / Type A) OX=289380 GN=pbpA PE=3 SV=1
P39793	2.94e-40	106	521	77	451	Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 SV=1
P38050	3.81e-37	106	524	49	422	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999532	0.000483	0.000001	0.000000	0.000000	0.000001

TMHMM Annotations download full data without filtering help

start	end
60	82