CAZyme Information: MGYG000000304_01193

Basic Information

• Species: CAG-1427 sp900542525
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; CAG-1427; CAG-1427 sp900542525
• CAZyme ID: MGYG000000304_01193
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
716	MGYG000000304_13|CGC1	78047.38	8.8679

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000304	1613120	MAG	Sweden	Europe

• Gene Location: Start: 23; End: 2173 Strand: +

Full Sequence      

MGAAAAANEGISAQANDGTIVVALDPGHGGTDPGATSNGLKESDITWKIAQACKAELENY
QNVRVYMTRTQNETLSLIERVRRAAEQGATVFVSIHINSAAATSAHGAEVWYPNDSSYNK
DAHTTGKELSQKILDELTALGLSDRGIKTKDTQTNSKYPDGSVRDYYGVIANARERGIPG
IIVEHAFISNLEENRKLADDAFLRQLGQADARGIVKTFDLQRKGGAWQQQADGSWKYQYA
NGSYAVNAWVTDNKKQYWIDANGTMVTGVCAVDGKVYHFDSSGVLQMTAGWKQLNGNWYY
FTKSGAAQTGWVKSGSKWYYQDPGSGVMKTGWVDVSGKKYFLTASGAMRSSTGWFKDGGN
WYWITGSGAAATGWVKAKGKWYYLDPASAVMKTGWVDVSGKKYFLNSSGAMRTSGWFKDG
GNWYWITGSGAAAMGWAKVKGKWYYQDPSTAIMQTGWKQVGQEWYYLNANGDMKTGWFKQ
GSTWYYLKGSGAMAVGWQTVNGKQYYFDSDGKMFTGEHNIDGKPCFFDASGVFVGNGTPI
MGVAKTNAATMTNAFVRQLALMGKSYPSDVLGAGGAPDPATFCQIIYEEATAEGVRPEVV
WAQVMWETGWLQMGGDVKLSQYNFAGLGATGNGVAGAGFPDVRTGIRAQVQHLKCYASTD
ELNNEKVDPRWSNSLRGKAKLVEWLGIPENPFGTGWAASAEYGYNLRGIMKDKLGI

Enzyme Prediction     

No EC number prediction in MGYG000000304_01193.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	583	712	1.8e-17	0.9609375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
NF033930	pneumo_PspA	1.34e-66	290	506	444	635	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033930	pneumo_PspA	1.99e-58	329	513	442	621	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033930	pneumo_PspA	3.23e-58	273	502	449	650	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
cd02696	MurNAc-LAA	3.33e-57	21	215	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.
NF033838	PspC_subgroup_1	9.13e-55	329	513	485	665	pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT35925.1	1.61e-87	1	711	16	683
QGS10651.1	3.03e-85	1	711	16	679
AKU64594.1	3.10e-85	20	711	32	680
QQC44737.1	2.28e-84	20	711	32	680
QTU85010.1	1.95e-82	12	710	270	1003

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JWQ_A	7.13e-20	21	221	3	179	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4BIN_A	9.49e-17	17	218	171	393	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
4RN7_A	1.92e-16	22	219	6	183	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5EMI_A	1.38e-15	18	222	3	180	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
5J72_A	1.58e-14	22	217	454	636	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37134	8.79e-23	20	226	2	183	N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM PE=3 SV=1
O48471	1.28e-22	21	225	4	188	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
Q06320	2.29e-22	20	248	2	206	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
O51481	2.39e-16	581	714	70	196	Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
Q02114	3.87e-16	24	218	324	495	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 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
1.000008	0.000033	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000304_01193.