CAZyme Information: MGYG000001390_01802

Basic Information

• Species: Bacillus_O smithii
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_B; Domibacillaceae; Bacillus_O; Bacillus_O smithii
• CAZyme ID: MGYG000001390_01802
• CAZy Family: GT51
• CAZyme Description: Penicillin-binding protein 4

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
278		32073.68	8.0221

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001390	3224201	Isolate	not provided	not provided

• Gene Location: Start: 37501; End: 38337 Strand: +

Full Sequence      

MKTIFGYFFTAVLMALAIYFFYFANQEAQHVESFDKVVEKKIPIHSVDLSQESKFLDQNG
RTFLEIRNPYRIVVSNKDIPDFMKELFLQSEDRQFYEHGGIDAFAVLRAMIVNSHSHQIE
QGGSTITQQLARNLYLNYNKTFSRKLSEVFYAYELEKKLTKDQILNLYLNTIYFQNGVYG
VEAASQFYFQKSVKDLTKAQMAFLAAIPNNPSLYNPLTHFANTKKRQERLIDLMKKNGFL
TAEEAEAAKKEPITVNYPPPTLRLEAGASSDLCVFAER

Enzyme Prediction     

No EC number prediction in MGYG000001390_01802.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	61	235	7.2e-65	0.9830508474576272

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	5.36e-84	59	235	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.
COG5009	MrcA	1.44e-77	1	266	1	262	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG0744	MrcB	1.88e-77	1	259	15	265	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	2.59e-49	71	266	66	261	penicillin-binding protein 1a; Provisional
TIGR02071	PBP_1b	2.84e-44	71	255	147	335	penicillin-binding protein 1B. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AKP48269.1	7.68e-174	1	255	1	255
BCB05441.1	2.80e-83	1	256	1	256
QHE62945.1	3.94e-83	1	256	1	256
SNV12227.1	1.20e-79	2	256	3	259
QED49145.1	2.34e-79	1	253	1	254

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NB6_A	1.98e-46	55	248	4	197	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A	2.79e-46	55	248	4	197	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	1.54e-44	44	266	12	234	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	7.90e-41	44	257	13	226	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	1.98e-37	72	258	40	226	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
P40750	3.90e-69	24	256	27	261	Penicillin-binding protein 4 OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpD PE=1 SV=2
P38050	2.06e-50	39	249	40	245	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O66874	8.79e-45	51	255	43	247	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
Q07806	9.29e-44	44	266	39	261	Penicillin-binding protein 1A OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=mrcA PE=1 SV=2
Q1RKC5	4.91e-42	53	255	49	254	Penicillin-binding protein 1A OS=Rickettsia bellii (strain RML369-C) OX=336407 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
0.995013	0.004195	0.000656	0.000025	0.000014	0.000114

TMHMM  Annotations     

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