CAZyme Information: MGYG000004138_01636

Basic Information

• Species: QAMH01 sp900544245
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; QAMH01; QAMH01; QAMH01 sp900544245
• CAZyme ID: MGYG000004138_01636
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1041		112513.18	4.5261

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004138	1946641	MAG	United Kingdom	Europe

• Gene Location: Start: 43550; End: 46675 Strand: -

Full Sequence      

MNKRSLYGRMLLSFALVLSLSPLALLSTSVGSIGIADAAAFADNGEVKVVADGTHDGGVV
DGPHRVGSFELGTSEAIEEAPLGFVYFDEATPAAGTEQKIAIAVDDQGATVRSAALLYET
PSGEVRAVESQTCAGASTLFSLQVDDPGDYCLLEMQAQVETSGGQEKLTKIDLAENGEDC
SFEVKQDEGSALSAMAEDEAVAANESEEIETTIYALGVEGDVEAADDIDDALIVAQEASA
FAMARAAGLVIALDPGHGGNDSGAVGSGLKESDVNWKIAQACKAELENYAGVTVVLTRTQ
NECPTLYERVERAVNQGAKVFVSLHINSTERSSADGAEVYYPNGSSYNKAAHETGKQLSQ
NILDELTALGLQDRGIKVRNSENNSKYPDGSLRDYYGVIADAREMGIPGIIVEHAFITNP
EDNAKLKDDNFLKKLGMADAQGIAKTYGLNKGGWEHQSDGTWKFKKVDGSYSKGWEYING
SWYYLDPSTAVMKTGWQTIGNAKYYLNPSGAMQETGWLKQGNDWYWITASGAAATDWTLV
NGVWYYMDLASCKMQTTGWFKHKDDWYWITGSGAAATGWVLINGSWYYMDPTSCKMQTGW
TTVGSDRYYLHPSGAMQGGGWFKDGNDWYWITPSGAAAKGWAVAYGSWYYMDPTSCKMQT
GWTTVGSDRYYLHPSGAMQGGGWFKDGNDWYWITPSGAAAKGWAVAYGSWYYMDPTSCKM
QTGWTTVGSDRYYLHPSGAMQGGGWFKDGNDWYWITPSGAAAKGWAVAYGSWYYMDPTSC
KMQTGWKKLGSTWYYLHDSGVMATGWLKLGDTWYYLHGSGAMATGWLTLGEAKYYLDSSG
AMVTGERTIDGEQCFFESSGAFVGNGTPIMGASKTTVAAMTQAYERSGFAYPSTALGAGG
APNAATFCQMIYEESNAEGVRAEVIFAQIMNETGWLQFGGDVSINQFNFGGIGATGNGVP
GNSFKDVRTGIRAQVQHLKAYASTEPLKNTCVDPRFNYVSRGCAKFVEWLGIGDNPTGQG
WCAGSGYGAKLKDIMKRNLGI

Enzyme Prediction     

No EC number prediction in MGYG000004138_01636.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	908	1038	1.7e-18	0.96875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	5.32e-56	250	444	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	3.70e-54	451	710	442	659	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	1.77e-51	620	823	444	643	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	3.81e-51	451	648	485	682	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.
NF033930	pneumo_PspA	1.39e-49	557	772	443	659	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTU85010.1	3.42e-85	70	1035	109	1003
QQC44737.1	1.84e-66	244	1036	27	680
AKU64594.1	3.42e-66	244	1036	27	680
QCT35925.1	3.62e-66	244	1036	27	683
QGS10651.1	4.79e-64	244	1036	27	679

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JWQ_A	2.03e-19	250	445	3	174	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5EMI_A	1.33e-16	249	445	5	176	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4RN7_A	5.50e-16	253	443	8	178	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5J72_A	2.86e-14	246	446	449	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]
4BIN_A	4.88e-12	249	443	174	389	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O51481	5.15e-22	906	1035	70	192	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	8.15e-21	248	447	319	495	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
O48471	7.41e-19	253	451	7	185	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
Q06320	9.93e-19	251	451	4	179	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
P54525	1.35e-17	248	447	29	204	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3

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
0.009227	0.989285	0.000422	0.000557	0.000258	0.000219

TMHMM  Annotations     

start	end
13	35