CAZyme Information: MGYG000000076_01674

Basic Information

• Species: Roseburia intestinalis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia intestinalis
• CAZyme ID: MGYG000000076_01674
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1455	MGYG000000076_11|CGC2	157726.58	5.5092

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000076	4318260	Isolate	United Kingdom	Europe

• Gene Location: Start: 104062; End: 108429 Strand: +

Full Sequence      

MKKRILAVIMAVCVSMTALPADVRAAEDGAVQTESTQAMETSSAEEAAVTEEASETENDE
TETSSESETTETGESSETETGVMETEETAETETGAVETEEPAETETTKTESTETETAETE
TAETETEEPAETETIETESTETETETETETETETETVQAAEMNYMMVESPYVETPGTQNV
VLSLGTGNEQISDVILNYQNLTTGKTYQIKAAGREEDMIRFTMDFSENGQAGEYQITSVQ
FTQEKTKQEILLSDLGMDVRFGVNEQAETNPDQVLYDEDAYADVDADVVTMSEDGEIVSE
NTVENVLEQGISKAVIGSTDHLKGANSSVTVVLDPGHDGTHAGASAFGVQEADLTLKIAT
YCKEELSTYNGITVYMTRESASCPAGGGDNIACLDARANLAKNVGANVLVSFHLNTANGT
ARGVEVYYPNSNYNAQVGGNGQALAKKICDKLAALGLNYRGTLIRNASYDKYPDGSAADY
YGLIRRCKNNGIPGLIIEHAFLDNANDYYTYLSSDEKLKALGVADATAIAEYFGLTKGAK
TVTLNYTQSRADGSLRLKWTGLDNVDYYEIYRNTVNDTNYPKIDEVSDATSYIDDTVKAG
TKYYYLVRPVFNDGTAGEYSKPISGVALGKTNLTKIKAKSGKKITLTWKKVSKAEGYLIY
RQDSSDSKFYQIGTVKSGSTLTYTDTVKSNNKTYTYKVQAYNTNNGRQGVGAYSSTKSAK
TLAKAKITGITSSDEEVLKISWNKVSGAKGYIISRSTKKDSGYSEIDTVSGEKTTSYTDD
TVKAGKTYYYKVEAYNVNSGTKGYGGASDAVAGKTAKRTKITSIVSTNEKTLTIKWNKIT
GAYGYRIKRSTDEDGTYKVVKTIKSGNTTSYKDTSVKAGKTYYYTVETMVKTGDNICYSG
DSASVEGRTAKKTKIKYAVSNGSNQIEVNWGAVSGAYGYRIKRSTSKNGTYNVIATVNGK
NKTTYQDKNVKTAKTYYYKVETINKVNGKKGYSGDSAVVSAKTLKTTSITAVKATGSTSV
RLEWKAVDGASGYQIYRSTSKDSGYKKVGQVKGKNTKKYEDKTLEAGKTYYYQVRAYKSN
SAKNGVASFSKAQKAWTIKQVVFSQITSDSKNQVTLGWKKVSKAQGYDIYRSDESNSGFE
KIASISSGSTLTYTDKGVKSGNTYYYKIAATYKIKGSAGRGSYSKVTEVAVLKQGSISSI
TLGDNNVLNISWNSVANASGYELAGAVSEKGTYTTLQTSGATSFTHSNLVQGTTYYYKVR
AYKDLSNGIRMYGPWSAVKAKAAAHEIMGTSSVTVDQMVSYYNKRYTFPADTYRDKGADS
AEAFFKILKEEAEAEGVRADVLFAQVMLETGGLQFGGDVQPSQCNFGGLGAVGGGAAGET
FADVRTGLRAQVQHLKAYASTDGLNNACVDKRFQYVSRGTARYVEWLAIPQNPYGKGWAA
DADYGAKLLRIMNSL

Enzyme Prediction     

No EC number prediction in MGYG000000076_01674.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	1.06e-38	330	530	1	172	N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
pfam01520	Amidase_3	5.19e-34	331	529	1	172	N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
COG0860	AmiC	6.33e-26	330	535	44	230	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
COG3401	FN3	4.92e-14	945	1261	13	325	Fibronectin type 3 domain [General function prediction only].
COG3401	FN3	1.14e-12	656	985	7	328	Fibronectin type 3 domain [General function prediction only].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VCV20908.1	0.0	1	1455	1	1463
CBL07763.1	0.0	1	1455	1	1457
CBL13779.1	0.0	1	1455	1	1458
AEN97541.1	1.20e-105	162	1455	129	1783
QEI32622.1	3.41e-93	162	1455	67	1309

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J72_A	4.18e-16	300	522	423	626	ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630]
4RN7_A	1.75e-07	326	507	1	157	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O51481	2.19e-18	1305	1455	54	195	Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
O48471	6.98e-11	328	606	2	253	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
P37134	7.89e-10	329	539	2	181	N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM PE=3 SV=1
Q06320	3.57e-09	329	537	2	179	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000349	0.998789	0.000287	0.000196	0.000194	0.000159

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000076_01674.