CAZyme Information: MGYG000001988_01943

Basic Information

• Species: Marvinbryantia sp900550755
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Marvinbryantia; Marvinbryantia sp900550755
• CAZyme ID: MGYG000001988_01943
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
502		55119.23	9.2991

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001988	3989920	MAG	Spain	Europe

• Gene Location: Start: 39790; End: 41298 Strand: -

Full Sequence      

MAAKKKLFLIAGHGEGDPGACSIWGQEANYTRELAKLVKTAIGSRMSVTLYDTNKNCYAQ
SKKGNVPTYSDYDMTVEFHFNAKAKADPNGDGRFTGVGGYTHPNNAGRSIARAIVDRVVA
LGFREWLLDTSTGLLNLNRAQGQGAKYFLLETAFIDDGDDMKFYTARKEIFAQAIAQGIL
DGLGVKSTATQPKAEQYYRVRLTKDDEKSQLFAGTKAGALAVCKTKPGYSVFDPDMKCIY
TNNAKGLQASALKGLSEKEWIEKVGPLYTTDEKTSGILACVSLAQGILESGYGQTDLAQA
GNNLHGMKTNLSGNTWPGTTWDGSSKYTNESPEQDANGNQYMKKSDFRRYGCIEESIADH
SAYLLNAANGKKQRYAGLAGEKDYRKAAQIIKDGGYATDTKYVSKLVNIIEKWNLTRYNA
SGSGSTPKPSAAEDEWKVPFLINTTCDWLWIRKGPAKKYDTSGHIAEKDGEKKKYTIVEV
KNGWGRLKSGIGWICLDYVKKV

Enzyme Prediction     

No EC number prediction in MGYG000001988_01943.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	266	415	2.1e-25	0.9765625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1705	FlgJ	9.44e-36	261	423	47	192	Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].
NF038016	sporang_Gsm	1.48e-19	261	418	164	311	sporangiospore maturation cell wall hydrolase GsmA. The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.
PRK06347	PRK06347	3.12e-19	247	433	139	331	1,4-beta-N-acetylmuramoylhydrolase.
cd02696	MurNAc-LAA	2.76e-17	6	180	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.
PRK08581	PRK08581	5.36e-16	277	419	340	472	amidase domain-containing protein.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADB89215.1	5.46e-74	246	497	199	440
QQQ98955.1	7.18e-74	242	496	198	446
AMP42248.1	5.70e-73	242	497	196	451
CBL18646.1	8.40e-69	244	502	190	505
AUV56483.1	8.08e-61	247	500	1	233

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FI7_A	3.71e-12	273	419	46	183	CrystalStructure of the autolysin Auto (Lmo1076) from Listeria monocytogenes, catalytic domain [Listeria monocytogenes EGD-e]
5T1Q_A	5.25e-12	230	419	35	212	ChainA, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_B Chain B, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_C Chain C, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_D Chain D, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O32083	5.28e-17	277	439	68	225	Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1
P37710	2.15e-11	256	424	179	338	Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2
P39046	3.53e-11	273	425	78	220	Muramidase-2 OS=Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R) OX=768486 GN=EHR_05900 PE=1 SV=1
Q2G222	5.87e-11	230	419	295	472	N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=SAOUHSC_02979 PE=1 SV=1
Q9CIT4	2.09e-08	256	426	61	221	Probable N-acetylmuramidase OS=Lactococcus lactis subsp. lactis (strain IL1403) OX=272623 GN=acmA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000061	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001988_01943.