CAZyme Information: MGYG000000944_00283

Basic Information

• Species: CAG-1427 sp900538545
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; CAG-1427; CAG-1427 sp900538545
• CAZyme ID: MGYG000000944_00283
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
927	MGYG000000944_2|CGC2	99967.39	4.9384

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000944	1785315	MAG	United Kingdom	Europe

• Gene Location: Start: 80404; End: 83187 Strand: +

Full Sequence      

MKSISNSLSRQVFQVVLSIVLVVSLMPALVHSAYADEIEDTQSSSEVTEQAAADQTSSKA
ETQALGFVYFEEADLIAGAPQKVAIAIDNDAITIGSAVLTYQDPTGAQHELSVEKCADSA
ALFTLQTEGAGTYQLLSMVAQVTTASGEQKTYSLDLAKEGANCAFEAQQDTGMALSTQSE
TEEASDGDMSIYALNDEGELEGTSDLDAAAGIVAAAAAEEGISAQANDGTIVVALDPGHG
GTDPGASSNGLNEADVNWKIAQACKAELEKYQNVRVYMTRTQNELPGLTERVRRAAEQGA
TVFVSIHINSAAATSAHGAEVWYPNDSSYNKDAHTTGKELSQKILNELTALGLSDRGIKT
KDTQTNSKYPDGSVRDYYTVIANARERGIPGIIVEHAFISNPEENKKLADDAFLRQLGQA
DARGIVKTFDLQRKGGAWQQQADGTWKYQYTNGSYAVNTWVTDNKKQYWIDANGTMVTGV
CAVEGKVYHFDSSGVLQTTAGWKQLNGNWYYFTKSGAAQTGWVKSGGKWYYQDPASGVMK
TGWVDVSSKKYFLTASGAMRSSTGWFNDGGNWYWITGSGAAATGWVKSGGKWYYQDPATA
IMKTGWVDVSGKKYFLNSSGAMRTSGWFKQDAGWYWITGSGAAATGWAKVKSKWYYLDPA
SALMKTGWQKVDDAWYYLNANGDMKTGWFKQGSTWYYLKGSGAMAVGWQTVNGKQYYFDA
DGKMLTGEHNIDGKPCFFEASGAFIGNGTPIMGVAKTNAATMTNAFVRQLALMGKSYPSD
VLGAGGAPDPATFCKIIYEEATAEGVRPEVVWAQVMWETGWLQMGGDVKLSQYNFAGLGA
TGNGVAGAGFPDVRTGIRAQVQHLKCYACTDALNNDRVDPRWSSSLRGKAKLVEWLGIPE
NPFGTGWAASAEYGYNLRGLMKDKLGI

Enzyme Prediction     

No EC number prediction in MGYG000000944_00283.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	794	923	2.5e-16	0.9609375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
NF033930	pneumo_PspA	7.14e-67	501	722	444	657	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	1.29e-57	232	426	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.
NF033930	pneumo_PspA	5.68e-55	563	743	443	620	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.
NF033838	PspC_subgroup_1	9.27e-54	517	723	483	681	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.
pfam01520	Amidase_3	1.93e-51	233	425	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTU85010.1	5.93e-103	60	921	111	1003
QCT35925.1	7.63e-82	213	922	14	683
AKU64594.1	1.89e-81	231	922	32	680
QQC44737.1	1.33e-80	231	922	32	680
QGS10651.1	1.26e-79	213	922	14	679

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4RN7_A	1.04e-18	233	430	6	183	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
1JWQ_A	2.87e-16	232	432	3	179	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5EMI_A	2.53e-15	229	427	3	176	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4BIN_A	2.47e-14	228	429	171	393	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A	1.31e-12	233	434	7	229	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37134	2.17e-20	231	437	2	183	N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM PE=3 SV=1
O48471	4.22e-20	232	436	4	188	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
Q06320	2.14e-18	231	433	2	179	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
Q9K0V3	8.50e-17	232	427	191	406	N-acetylmuramoyl-L-alanine amidase AmiC OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=amiC PE=1 SV=1
Q02114	1.04e-15	235	429	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.041432	0.955915	0.000895	0.000705	0.000488	0.000537

TMHMM  Annotations     

start	end
12	34