CAZyme Information: MGYG000000462_01527

Basic Information

• Species: UBA940 sp900768115
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; UBA940; UBA940 sp900768115
• CAZyme ID: MGYG000000462_01527
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
343		38550.41	9.7771

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000462	1821707	MAG	Fiji	Oceania

• Gene Location: Start: 6876; End: 7907 Strand: -

Full Sequence      

MTKNMRKTILTLLGVLAFAESFGQWTTNTLRRKDIPRTPVDTVATKRDDVKIVVYADNTF
SYLYTAAEELQQSEIYREHWDTANVFSYKSISYQSLPETVDVRLIGSLDEFRVPLTGTII
SRYGPRGRRNHNGVDVPLKTGAPIAAAFDGRVRYSRYNSGGFGNLVIVRHPNGLETYYGH
LSRRNVKAGDWVVAGQIIGYGGSTGRSRGPHLHFEVRYCDQTFDPQRIIDFQSGSLRYQT
FVLEKSFFNIRSRATEGLEDGDDFDVNAFIAQNGGKTDEEISAAIAQEEKKAAEPVMAYH
TVRSGETLSSIARRNGTTVDNLCRLNGMTRNSVLRIGRKLRVK

Enzyme Prediction     

No EC number prediction in MGYG000000462_01527.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	7.14e-43	129	225	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.
COG0739	NlpD	6.13e-39	117	231	143	263	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	2.88e-38	131	216	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.
COG4942	EnvC	2.29e-19	66	227	260	416	Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].
PRK11649	PRK11649	6.31e-18	114	225	305	406	putative peptidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCG55335.1	1.18e-111	27	343	33	362
QGA22752.1	1.37e-111	29	343	34	356
CDN32287.1	3.53e-91	33	343	44	356
AFL79509.1	6.89e-89	40	343	63	348
BBL02665.1	2.27e-86	40	343	71	356

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J1L_A	2.17e-24	130	225	64	160	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	5.75e-20	129	225	244	338	Crystalstructure of NMB0315 [Neisseria meningitidis ATCC 13091],3SLU_B Crystal structure of NMB0315 [Neisseria meningitidis ATCC 13091]
6MUK_A	7.41e-20	129	225	264	358	1.93Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae. [Neisseria gonorrhoeae FA 1090]
5J1L_B	2.55e-17	121	248	27	168	Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_D Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_B Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_D Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]
5J1K_A	4.38e-17	121	248	46	187	Crystalstructure of Csd2-Csd2 dimer [Helicobacter pylori 26695]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A0H3C9Q9	2.02e-18	110	230	481	602	Cell division protein DipM OS=Caulobacter vibrioides (strain NA1000 / CB15N) OX=565050 GN=dipM PE=3 SV=1
P44693	1.34e-16	112	225	338	442	Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 SV=1
O05156	9.47e-15	130	215	149	235	Glycyl-glycine endopeptidase ALE-1 OS=Staphylococcus capitis OX=29388 PE=1 SV=1
P45682	2.46e-14	114	225	181	290	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
P10548	6.67e-14	131	215	266	351	Lysostaphin OS=Staphylococcus staphylolyticus OX=1287 GN=lss 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
0.067697	0.908455	0.022852	0.000385	0.000298	0.000291

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000462_01527.