CAZyme Information: MGYG000004136_00612

Basic Information

• Species: Eisenbergiella sp900555195
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900555195
• CAZyme ID: MGYG000004136_00612
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
405	MGYG000004136_10|CGC2	43284.82	4.8331

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004136	3901051	MAG	United Kingdom	Europe

• Gene Location: Start: 21592; End: 22809 Strand: -

Full Sequence      

MRINVHAGHNPDGMVACGAIGLIRESTEARAVKDRVIAQLVSMGHTVRDCTCNNGISQND
ILQKIVAACNAQEADLDISIHFNAGAQPEADGHTTGTEVYVYSTSSVSAAYAQQVVDSIA
ALGFRNRGIKERPSLYVLRHTKAPAMLIECCFVDDPEDVALYNADRMAAAIVAGITGQAS
ETTADAAKLAAMSQAEFVDWIGQLAAVDMRTSGILASVTAAQSILESGYGKSELALNALN
LGGMKAELSGNTWPSAWDGKIYTKDTAEQEPDGTYITIKADFRAYPSVAAYLADHSAYLA
GAETGGKLRYAGIVGCKDYRQAFQILKDGGYATSLDYVDKLCAVVEKWNLTRYDGATPIG
QSEIYWLSAADVFTEAEADAVKVQLEAAWPGLNLLKRRGIVTKAY

Enzyme Prediction     

No EC number prediction in MGYG000004136_00612.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	203	350	7.9e-23	0.9765625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	4.39e-41	2	176	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.
COG1705	FlgJ	2.97e-37	180	363	29	197	Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].
pfam01520	Amidase_3	3.35e-30	6	175	7	172	N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
NF038016	sporang_Gsm	1.86e-25	184	354	150	312	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.
COG0860	AmiC	9.17e-23	6	175	51	224	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADB89215.1	1.21e-62	167	362	181	380
QBF75599.1	4.59e-61	192	356	1	165
QQQ98955.1	8.63e-58	162	357	178	377
AMP42248.1	2.03e-56	186	354	203	373
CBL18646.1	3.51e-55	201	354	210	365

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1XOV_A	6.03e-17	18	214	28	217	ChainA, Ply protein [Listeria phage PSA]
2ZYC_A	8.49e-11	192	345	1	144	ChainA, Peptidoglycan hydrolase FlgJ [Sphingomonas sp. A1]
3VWO_A	1.32e-10	197	345	4	143	Crystalstructure of peptidoglycan hydrolase mutant from Sphingomonas sp. A1 [Sphingomonas sp. A1]
3K3T_A	5.35e-10	192	345	1	144	E185Amutant of peptidoglycan hydrolase from Sphingomonas sp. A1 [Sphingomonas sp. A1]
3FI7_A	3.09e-09	194	354	30	183	CrystalStructure of the autolysin Auto (Lmo1076) from Listeria monocytogenes, catalytic domain [Listeria monocytogenes EGD-e]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O32083	2.12e-19	194	388	48	237	Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1
P58698	8.49e-19	1	163	1	158	Uncharacterized protein CPE1502 OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=CPE1502 PE=4 SV=1
P18020	7.09e-16	1	163	1	158	Uncharacterized 38.4 kDa protein OS=Clostridium perfringens OX=1502 PE=4 SV=1
P39046	4.22e-08	190	354	58	214	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
Q9CIT4	1.00e-07	181	362	49	222	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
1.000057	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004136_00612.