CAZyme Information: MGYG000002101_00708

Basic Information

• Species: Sutterella seckii_A
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Sutterella; Sutterella seckii_A
• CAZyme ID: MGYG000002101_00708
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
300		31235.86	10.0968

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002101	2568007	MAG	Mongolia	Asia

• Gene Location: Start: 28634; End: 29536 Strand: -

Full Sequence      

MRVLSRSRTGFILSAAALVLAGCSSLPPGEVPIVNRNVASGSSTALDSPMKLGGVSDSGA
THTVAPGDTIYNISQRYGVNASDLMQMNAITDPTTLRLGQVLRLPRATRAPVTTASSAVK
IHRLEAQAPIETATVITPAETSSSEPVIKAAEEKTPEAKPAVEEAKTPEKKEAPAVIPGT
RFLWPARGPILSDYAKNGKGLDIGGTAGSVVVAAGAGQILFVGGGVKGYGNLVIVKHTPT
LVTAYGHNSKVVVKPGDQVKAGQKIAEMGSTDADRVMLRFEVRDKGQPVDPMKYLPPARQ

Enzyme Prediction     

No EC number prediction in MGYG000002101_00708.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10871	nlpD	1.80e-45	13	296	16	317	murein hydrolase activator NlpD.
COG0739	NlpD	1.13e-44	61	299	3	268	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	3.24e-32	199	291	4	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.
COG4942	EnvC	7.39e-25	120	291	239	414	Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].
cd12797	M23_peptidase	1.22e-24	199	282	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDA55742.1	4.48e-182	1	300	1	295
QQS89964.1	8.43e-99	16	299	15	312
BBF24071.1	9.85e-90	17	299	36	323
QBR40763.1	7.62e-52	15	296	16	285
AZV93835.1	1.07e-51	15	296	16	285

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BH5_A	1.81e-15	178	295	17	140	LytMdomain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_B LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_C LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_D LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12]
6TPI_A	4.30e-14	178	295	261	384	EnvCbound to the FtsX periplasmic domain [Escherichia coli K-12]
5J1L_A	1.80e-08	189	294	57	163	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]
4UZ2_A	2.14e-08	60	109	3	51	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	1.15e-06	60	109	3	51	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
P45682	1.80e-46	19	296	34	295	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
Q46798	7.07e-40	58	297	38	244	Uncharacterized lipoprotein YgeR OS=Escherichia coli (strain K12) OX=83333 GN=ygeR PE=3 SV=2
P44833	1.72e-34	59	296	144	403	Outer membrane antigenic lipoprotein B OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=lppB PE=3 SV=1
P0ADA3	2.17e-33	58	296	119	377	Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1
P0ADA4	2.17e-33	58	296	119	377	Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000002	1.000013	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002101_00708.