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CAZyme Information: MGYG000002343_00204

You are here: Home > Sequence: MGYG000002343_00204

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Acinetobacter courvalinii
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter courvalinii
CAZyme ID MGYG000002343_00204
CAZy Family CBM50
CAZyme Description Murein hydrolase activator NlpD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
276 MGYG000002343_1|CGC2 29252.55 10.4747
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002343 4074146 Isolate United States North America
Gene Location Start: 197022;  End: 197852  Strand: +

Full Sequence      Download help

MHLNHVSVFL  SQKMIKTIVL  SMAVATVAVM  TGCASKPQVN  GGARHTLPAP  NYYTVRSGDT60
LSGISNRYGL  NYLNVAALND  IAPPYRIYVN  QSLRLKGSAA  QRTTSTQAMA  QTAPIQRQSI120
NLPSQQPVAP  KPQPVVPRPV  VPTVPVNPSS  STVASSLRWV  KPSNGAVIQT  FNLASNVKGT180
RYGGNVGDPI  FAAANGQVVY  AADGLKEYGN  LVLVKHIDGY  ITAYAHNSKM  LVKSGDNVTA240
GQKIAEMGSS  GASQVMLEFQ  VRLDGKPVNP  STVLPN276

Enzyme Prediction      help

No EC number prediction in MGYG000002343_00204.

CDD Domains      download full data without filtering help

Created with Snap1327415569829611012413815116517919320722023424826251275nlpD50276NlpD178270Peptidase_M23178261M23_peptidase149272EnvC
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10871 nlpD 9.96e-45 51 275 61 317
murein hydrolase activator NlpD.
COG0739 NlpD 4.73e-33 50 276 1 266
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 1.84e-32 178 270 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.
cd12797 M23_peptidase 2.04e-24 178 261 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.
COG4942 EnvC 2.23e-23 149 272 287 416
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits      help

Created with Snap132741556982961101241381511651791932072202342482621276QHH96367.1|CBM501276QHH94756.1|CBM501276AZM38622.1|CBM501276AVZ85437.1|CBM501276APR69909.1|CBM50
Hit ID E-Value Query Start Query End Hit Start Hit End
QHH96367.1 1.08e-164 1 276 1 274
QHH94756.1 1.03e-162 1 276 1 274
AZM38622.1 6.12e-160 1 276 1 276
AVZ85437.1 1.23e-159 1 276 1 276
APR69909.1 3.75e-154 1 276 1 276

PDB Hits      download full data without filtering help

Created with Snap132741556982961101241381511651791932072202342482621782704BH5_A1782706TPI_A1862705J1L_A1562715KVP_A1792696UE4_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BH5_A 3.21e-12 178 270 44 136
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 4.04e-11 178 270 288 380
EnvCbound to the FtsX periplasmic domain [Escherichia coli K-12]
5J1L_A 1.07e-10 186 270 74 160
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]
5KVP_A 1.90e-09 156 271 12 131
Solutionstructure of the catalytic domain of zoocin A [Streptococcus equi subsp. zooepidemicus]
6UE4_A 3.50e-09 179 269 268 358
ShyAEndopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961],6UE4_B ShyA Endopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961]

Swiss-Prot Hits      download full data without filtering help

Created with Snap1327415569829611012413815116517919320722023424826228275sp|P45682|NLPD_PSEAE16275sp|Q46798|YGER_ECOLI53275sp|P39700|NLPD_SALDU53275sp|Q56131|NLPD_SALTI53275sp|P40827|NLPD_SALTY
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P45682 1.94e-41 28 275 33 295
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 1.10e-38 16 275 9 243
Uncharacterized lipoprotein YgeR OS=Escherichia coli (strain K12) OX=83333 GN=ygeR PE=3 SV=2
P39700 1.98e-36 53 275 121 375
Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
Q56131 2.57e-36 53 275 117 371
Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P40827 2.77e-36 53 275 121 375
Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000668 0.006690 0.992545 0.000095 0.000023 0.000011

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002343_00204.