CAZyme Information: MGYG000000176_01611

Basic Information

• Species: Muricomes oroticus
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Muricomes; Muricomes oroticus
• CAZyme ID: MGYG000000176_01611
• CAZy Family: GT51
• CAZyme Description: Penicillin-binding protein 1F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
235	MGYG000000176_5|CGC5	26789.57	6.2612

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000176	5921397	Isolate	China	Asia

• Gene Location: Start: 171468; End: 172175 Strand: -

Full Sequence      

MKLIRRFLAFIFLCILCAGCFIGYRGYERYRQVLETESLQEKVAEIKNNPSYTTLDHLPQ
IYLDAVVAVEDKRFYKHPGIDPISIARAIKNDIQAWELIEGGSTITQQLAKNLYFNQERS
ITRKAAEGFMALKIEREYSKKEILELYVNSIYFGGGYYCIADASRGYYGKEPAEMTDYES
TMLAGIPNAPSVYAPDVNPDLAHSRQQKVLQSMINQKYITQEESSRIANAGETAF

Enzyme Prediction     

No EC number prediction in MGYG000000176_01611.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	43	213	3.1e-61	0.9661016949152542

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	1.19e-80	49	213	12	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	3.32e-78	52	223	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	3.34e-69	64	223	90	250	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	5.23e-68	1	223	2	240	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG4953	PbpC	2.46e-51	53	229	61	236	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
QUO38940.1	1.39e-91	1	227	1	231
QRP41835.1	5.54e-87	9	233	12	236
ASN93505.1	5.54e-87	9	233	12	236
QIX92252.1	1.11e-86	9	233	12	236
ANU46909.1	1.11e-86	9	233	12	236

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	1.83e-47	52	229	22	199	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	7.30e-47	52	229	22	199	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
5U2G_A	4.97e-36	55	223	45	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]
3UDF_A	1.80e-34	58	223	47	212	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	4.93e-34	35	222	26	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38050	8.90e-43	21	224	32	241	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O66874	9.52e-43	52	229	65	242	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
O87626	8.49e-42	52	223	70	241	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
O87579	1.59e-41	52	229	70	247	Penicillin-binding protein 1A OS=Neisseria lactamica OX=486 GN=mrcA PE=3 SV=1
O86088	1.59e-41	52	229	70	247	Penicillin-binding protein 1A OS=Neisseria cinerea OX=483 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
0.079187	0.000525	0.920289	0.000003	0.000003	0.000021

TMHMM  Annotations     

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