CAZyme Information: MGYG000002314_02033

Basic Information

• Species: Brevibacillus_C massiliensis
• Lineage: Bacteria; Firmicutes; Bacilli; Brevibacillales; Brevibacillaceae; Brevibacillus_C; Brevibacillus_C massiliensis
• CAZyme ID: MGYG000002314_02033
• CAZy Family: CBM50
• CAZyme Description: Murein hydrolase activator NlpD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
303	MGYG000002314_43|CGC1	33870.2	5.9135

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002314	4952787	Isolate	France	Europe

• Gene Location: Start: 97828; End: 98739 Strand: +

Full Sequence      

MMDAYAADTQVPWQSSDEARQAVVEQSLLQAFNPYTIFEEEEELPQKRSPVISYTVQQGD
TLSEIAYRNGISLKELVEQNKIKNPNFVGIGLKLTMKRNEIIHTVGSGETLDQIAARYQV
SESAIAARNPLVRLIPDNLYIGQVLYVPIPLQRRMPAGHEDIAERSSVQVASRGTLRSRT
MEWPIENATITSDFGSRWGRMHKGIDLWNENKGNTPILAAKSGTVIEAGTTRAGYGQLVV
LDHGDGLNTFYAHMRKILVTVGQEVNQGDVLGYMGNTGDSTNYHLHFEVRQDDTPVNPLR
FLR

Enzyme Prediction     

No EC number prediction in MGYG000002314_02033.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0739	NlpD	5.75e-48	54	303	4	265	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	1.17e-42	200	298	1	96	Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
cd12797	M23_peptidase	1.14e-36	202	289	1	85	M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
PRK10871	nlpD	2.58e-23	53	302	62	316	murein hydrolase activator NlpD.
PRK11649	PRK11649	1.62e-19	172	299	280	407	putative peptidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AKF93901.1	9.97e-123	2	303	1	301
AUM67048.1	4.14e-117	2	303	1	301
AIG28722.1	1.18e-116	2	303	1	301
QIC06771.1	1.18e-116	2	303	1	301
AYK05906.1	1.18e-116	2	303	1	301

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J1L_A	1.09e-21	202	303	65	165	Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_C Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_A Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_C Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]
3SLU_A	8.15e-16	184	299	222	339	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	9.54e-16	184	299	242	359	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5KVP_A	2.76e-15	178	298	12	130	Solutionstructure of the catalytic domain of zoocin A [Streptococcus equi subsp. zooepidemicus]
6JMX_A	4.76e-15	187	302	128	246	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45682	2.13e-24	47	302	60	294	Lipoprotein NlpD/LppB homolog OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=PA3623 PE=3 SV=1
P39700	1.32e-23	53	302	120	374	Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
Q56131	1.73e-23	53	302	116	370	Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P40827	1.81e-23	53	302	120	374	Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2
P0ADA3	3.51e-23	53	302	122	376	Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD 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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002314_02033.