CAZyme Information: MGYG000003113_00442

Basic Information

• Species: Pauljensenia sp001838165
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Pauljensenia; Pauljensenia sp001838165
• CAZyme ID: MGYG000003113_00442
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
686	MGYG000003113_3|CGC2	73880.91	4.6924

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003113	2324284	MAG	United States	North America

• Gene Location: Start: 41728; End: 43788 Strand: +

Full Sequence      

MRSSWRTIVAGLTLALGAAAAALVPPAHAAGITIAIDPGHGGSDSGAVANGLREKDLTLA
VSLALKEELESYDGVRVVMTRTTDTRPSENVSTDLSSRVDMAAAADADALVSIHFNSASP
IAKGAEVWYANSSSYNYGTHTQGRTLANAIQKQLTGLGLADRGIKTRDNPYYDYPDGSTG
DYYAIIRQAREENMTGVIVEHAFVTSTSDAALLRDESFVRSLGIADATGIAQAYGLSKGS
WRAVGDSWSFISNGTAKTGWFSAGGRWYWAGSDERTIRGWSTINGRRYFFDDSTAMVTGW
KQEDGKWYYLRPDGDMATGWVKVAGSWYYMNADGVMVTGWLKDGNDWYWLRADGAAAIGW
ANVDGAWYLFEDDARMLTGWQLTEDDNRWYYMRPSGQMVTGWLLDGGKWYYLDGDGAMVT
GWTKVGDTWYHLGSSGAMSTGWLLDGAWYWLDPNSGAMATGTVTVEGRASTFASSGAWLG
YADGSDAQAASRSASRSASVTNAAGQRLIMSAPTASRSEVIDAMEEAWDEAGYSYPSALS
AGGAQTIRDFASIIYDEAVAEGVSPELVFVQAMKETGWLRFGGDVTVSQYNFSGIGAVGG
GAKGASFPDVRTGIRAQVQHLRAYADSSVTTASLANPVVDPRFTYVRKGTAPVVEYLGIQ
ENPNRTGWAAAKNYGYDLVSMMKAYF

Enzyme Prediction     

No EC number prediction in MGYG000003113_00442.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	553	685	1.2e-18	0.953125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
NF033930	pneumo_PspA	1.01e-68	255	467	440	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.
NF033838	PspC_subgroup_1	2.32e-62	255	454	483	679	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	4.18e-61	238	446	442	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.
NF033838	PspC_subgroup_1	1.57e-60	298	485	486	662	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.
cd02696	MurNAc-LAA	2.98e-50	33	231	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT35925.1	1.38e-313	1	686	1	686
QGS10651.1	3.93e-300	1	686	1	682
AKU64594.1	3.72e-249	1	686	1	683
QQC44737.1	3.02e-248	1	686	1	683
ARD41193.1	6.56e-78	462	686	186	389

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J72_A	3.22e-17	29	230	449	633	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]
1JWQ_A	2.36e-13	34	226	4	170	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A	9.67e-13	33	232	5	176	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5EMI_A	4.37e-11	32	230	5	174	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
7RAG_B	1.72e-09	33	238	18	213	ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O48471	1.37e-21	36	240	7	187	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
P54525	1.78e-20	1	234	1	204	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q06320	7.92e-19	32	257	2	209	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
P37134	6.36e-18	32	238	2	179	N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM PE=3 SV=1
O51481	1.44e-17	547	682	68	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

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
0.000435	0.998726	0.000183	0.000230	0.000201	0.000181

TMHMM  Annotations     

start	end
7	29