CAZyme Information: MGYG000000446_01434

Basic Information

• Species: UMGS1045 sp900547995
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; UMGS1045; UMGS1045 sp900547995
• CAZyme ID: MGYG000000446_01434
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
229	MGYG000000446_39|CGC1	26423.01	9.9088

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000446	1423737	MAG	Sweden	Europe

• Gene Location: Start: 4869; End: 5558 Strand: -

Full Sequence      

MKLVKKIAITILLIFICIGSYFICSGYQMYKNALNKMPLKDKITTIRPKEDYTKIDDMPQ
IYLKAVVSVEDHRFYKHFGIDVISIGRAFVNNIKKMKFVEGGSTITQQLAKNIYFTQDKK
IVRKVAEIFMAFSIESNYNKDEILELYLNTSYYGNGFYSVKSASLGYFNKLPKDMNDSES
IMLAGIPNAPSLYNPIQNKNLAIERQRQVINKMIKYGNLDKVETEKIIK

Enzyme Prediction     

No EC number prediction in MGYG000000446_01434.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	47	213	7.2e-61	0.9378531073446328

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	2.30e-79	47	213	10	176	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	1.89e-75	52	229	4	181	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	1.93e-67	43	217	69	244	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	5.22e-66	1	229	2	246	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG4953	PbpC	8.73e-44	53	227	61	234	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
QJU22158.1	1.46e-85	4	217	7	220
QRP41835.1	5.90e-85	4	217	7	220
ASN93505.1	5.90e-85	4	217	7	220
QIX92252.1	2.24e-82	4	217	7	220
ANU46909.1	9.08e-82	4	217	7	220

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	6.90e-43	49	228	19	198	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	2.75e-42	49	228	19	198	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
4OON_A	2.03e-38	57	220	46	209	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	1.49e-34	58	228	47	217	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	1.96e-33	32	229	2	219	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
O05131	6.97e-42	49	214	67	232	Penicillin-binding protein 1A OS=Neisseria gonorrhoeae OX=485 GN=mrcA PE=1 SV=3
P0A0Z6	6.97e-42	49	214	67	232	Penicillin-binding protein 1A OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=mrcA PE=3 SV=1
P0A0Z5	6.97e-42	49	214	67	232	Penicillin-binding protein 1A OS=Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) OX=122587 GN=mrcA PE=3 SV=1
Q5FAC7	6.97e-42	49	214	67	232	Penicillin-binding protein 1A OS=Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) OX=242231 GN=mrcA PE=3 SV=3
O87626	9.54e-42	49	229	67	247	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA 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
0.441601	0.046532	0.509656	0.000267	0.000160	0.001791

TMHMM  Annotations     

start	end
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