CAZyme Information: MGYG000004691_00840

Basic Information

• Species: UBA9502 sp900555625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA9502; UBA9502 sp900555625
• CAZyme ID: MGYG000004691_00840
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
245	MGYG000004691_21|CGC1	27578.41	8.5472

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004691	2701187	MAG	China	Asia

• Gene Location: Start: 16922; End: 17659 Strand: -

Full Sequence      

MRLRKLTGWMTATALTVMSCTGFTVLKEGYETYQTAVEAESLDEKIAKIQAKRGYTKLSE
LPDTYAQAVVSVEDHRFYNHFGLDPIAIGRALVRDLKARRYVEGGSTITQQLAKNLYFSQ
EKQLSRKVAEVFLALDLEQKYSKDEILELYVNSIYYGDGYQNIGQASRGYFGKEPSKMSD
YECTLLAGVPNAPSRYAPSKHPDLASKRQQKVLSRMQVCGYLTKEETSEVNAQILALNLH
FVGAN

Enzyme Prediction     

No EC number prediction in MGYG000004691_00840.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	45	217	5.3e-62	0.9774011299435028

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	3.30e-81	50	217	10	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	2.30e-77	52	239	1	188	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	4.05e-69	49	238	72	262	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	8.80e-67	52	241	66	255	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	1.33e-49	34	240	45	253	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRP41835.1	2.75e-92	1	232	1	232
ASN93505.1	2.75e-92	1	232	1	232
QJU22158.1	7.86e-92	1	232	1	232
ANU46909.1	1.29e-90	1	232	1	232
QQQ98385.1	1.29e-90	1	232	1	232

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	9.87e-50	52	229	19	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]
3NB6_A	3.95e-49	52	229	19	196	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
4OON_A	5.47e-37	50	225	36	211	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]
3UDF_A	5.84e-36	60	239	46	225	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	3.20e-33	50	240	37	227	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	3.91e-45	43	240	57	252	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O66874	8.03e-45	52	229	62	239	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
P39793	1.88e-43	45	226	86	269	Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 SV=1
Q9KNU5	1.12e-40	34	240	45	253	Penicillin-binding protein 1A OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=mrcA PE=3 SV=2
Q00573	3.20e-40	43	226	60	247	Penicillin-binding protein 1A (Fragment) OS=Streptococcus oralis OX=1303 GN=ponA PE=3 SV=1

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
0.000000	0.000010	1.000059	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004691_00840.