CAZyme Information: MGYG000004847_00497

Basic Information

• Species: UMGS1670 sp902406135
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Anaerotignaceae; UMGS1670; UMGS1670 sp902406135
• CAZyme ID: MGYG000004847_00497
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
565	MGYG000004847_3|CGC1	61063.24	7.6177

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004847	2381643	MAG	China	Asia

• Gene Location: Start: 41167; End: 42864 Strand: +

Full Sequence      

MKISVKLTRAENTALLGAGPVELDLEEYLCGVVPSEIYESSHMEALKAQAVAARTFAVRR
AMAGTVVDDTTSFQAYRAPLAESSPRSRQAVEETAGQVLTYGGEVIDCFYSASNGGTCKR
SGEVWSRDYPYYVNKPDPWDTAARTEKPTNPSHGVGLSQVGCMWAAKQGVPYNEILAFYY
SGAALVHEYGTGSVVGFEEETGGFAMNLHTLIFTNNACYKAGRKITPKGIMVHSTGANNP
WLKRYVGPDDGLLGKNQYNNHWNQPMDREVCVHAFIGKLADGTIATYQTLPWDHRGWHCG
SGSKGSGNNTHISFEICEDGLTDSAYFNKVYNEAVELCAYLCKQYGLTEKNIICHSEGHA
QGIASNHGDVMHWFPKHGKNMDTFRAAVKAKLAGSSSGNTGGSAGNGTLYRVRKSWSDAS
SQLGAFAVLDNAKELADKNPGYAVFDEAGKKVYPSASGSTGSGTLYRVRKSWADAASQKG
AFNVLDNAKRCADENPGYSVFDEAGKVVYAGSAAASTYTVQKGDSLWAIAEKRLGNGTRY
NEIKKLNGLTSDVIYAGQVLKLPNR

Enzyme Prediction     

No EC number prediction in MGYG000004847_00497.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02669	SpoIID_LytB	1.41e-45	22	186	5	266	SpoIID/LytB domain. This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General]
COG2385	SpoIID	7.76e-35	24	185	143	390	Peptidoglycan hydrolase (amidase) enhancer domain [Cell wall/membrane/envelope biogenesis].
pfam08486	SpoIID	2.21e-29	22	100	10	100	Stage II sporulation protein. This domain is found in the stage II sporulation protein SpoIID. SpoIID is necessary for membrane migration as well as for some of the earlier steps in engulfment during bacterial endospore formation. The domain is also found in amidase enhancer proteins. Amidases, like SpoIID, are cell wall hydrolases.
cd06583	PGRP	2.93e-24	227	357	2	115	Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.
pfam01510	Amidase_2	3.43e-17	226	357	1	112	N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEY67694.1	8.08e-152	206	563	1	296
CDM67796.1	1.18e-145	206	564	1	314
QAT44066.1	2.92e-139	206	564	1	317
AOT72278.1	4.67e-132	206	564	1	314
QAT50916.1	1.23e-127	206	563	1	306

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4RWR_A	3.94e-18	23	143	66	201	2.1Angstrom Crystal Structure of Stage II Sporulation Protein D from Bacillus anthracis [Bacillus anthracis],4RWR_B 2.1 Angstrom Crystal Structure of Stage II Sporulation Protein D from Bacillus anthracis [Bacillus anthracis]
5I1T_A	2.23e-11	22	140	63	200	ChainA, Stage II sporulation protein D [Clostridioides difficile 630]
5TXU_A	2.64e-11	22	140	87	224	ChainA, Stage II sporulation protein D [Clostridioides difficile 630]
4UZ2_A	1.41e-06	516	565	3	49	Crystalstructure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_D Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ3_A Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8]
4XCM_A	5.51e-06	514	565	1	49	Crystalstructure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4XCM_B Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q02113	7.55e-18	29	140	422	529	Amidase enhancer OS=Bacillus subtilis (strain 168) OX=224308 GN=lytB PE=1 SV=1
P13251	9.48e-14	3	140	61	211	Stage II sporulation protein D OS=Bacillus amyloliquefaciens OX=1390 GN=spoIID PE=4 SV=1
P07372	1.26e-13	3	149	60	219	Stage II sporulation protein D OS=Bacillus subtilis (strain 168) OX=224308 GN=spoIID PE=4 SV=1
C0QYX7	8.74e-10	22	131	106	219	Uncharacterized protein BHWA1_00569 OS=Brachyspira hyodysenteriae (strain ATCC 49526 / WA1) OX=565034 GN=BHWA1_00569 PE=1 SV=1
Q5HRU2	4.95e-06	455	563	75	191	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 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
1.000043	0.000013	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004847_00497.