CAZyme Information: MGYG000001577_00980

Basic Information

• Species: CAG-238 sp900542245
• Lineage: Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Anaerovoracaceae; CAG-238; CAG-238 sp900542245
• CAZyme ID: MGYG000001577_00980
• CAZy Family: GT51
• CAZyme Description: Penicillin-binding protein 1F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
226	MGYG000001577_34|CGC1	25477.12	5.6634

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001577	2356070	MAG	United States	North America

• Gene Location: Start: 13421; End: 14101 Strand: -

Full Sequence      

MKKLIGRLLAIVLIAALAVCGIVTYNGYQLYKEAVAAVPVSEKVAAIEAQTHYTTYDALP
KRYIEAVIAAEDRRFFRHHGFDILATGRAMWHNIEAGRLIEGGSTITQQLAKNMYFSQEK
KFTRKVAEVFVAQELEDLCDKKTLFELYVNSIYFGSGYYNIYDAAHGYYDKDPSDLNDYE
CTMLAGIPNAPSVYAPTVNPKLAEERRQQVLTCMVENGYITEGEIQ

Enzyme Prediction     

No EC number prediction in MGYG000001577_00980.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	48	214	3.9e-58	0.9378531073446328

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	1.41e-74	53	215	15	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	6.61e-72	53	224	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	3.26e-66	7	224	22	250	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	5.46e-65	1	224	1	240	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
TIGR02071	PBP_1b	3.32e-41	57	226	153	326	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
QRP41835.1	8.79e-79	10	222	12	224
ASN93505.1	8.79e-79	10	222	12	224
QJU22158.1	3.56e-78	10	222	12	224
QIX92252.1	1.01e-77	10	222	12	224
ANU46909.1	1.01e-77	10	222	12	224

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	1.39e-44	53	221	22	190	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	5.56e-44	53	221	22	190	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
3UDF_A	8.45e-39	56	226	44	214	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]
4OON_A	1.69e-35	59	226	47	214	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	4.51e-33	59	224	48	213	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
P38050	5.44e-45	2	224	7	240	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O87626	2.71e-40	48	221	65	238	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
O66874	4.02e-40	53	221	65	233	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
O87579	1.56e-38	48	221	65	238	Penicillin-binding protein 1A OS=Neisseria lactamica OX=486 GN=mrcA PE=3 SV=1
Q5FAC7	2.13e-38	48	221	65	238	Penicillin-binding protein 1A OS=Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) OX=242231 GN=mrcA PE=3 SV=3

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
0.200468	0.005556	0.793304	0.000023	0.000019	0.000622

TMHMM  Annotations     

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