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CAZyme Information: MGYG000001501_03408

You are here: Home > Sequence: MGYG000001501_03408

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 Bacillus_J andreraoultii
Lineage Bacteria; Firmicutes; Bacilli; Bacillales_B; Caldibacillaceae; Bacillus_J; Bacillus_J andreraoultii
CAZyme ID MGYG000001501_03408
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
198 21429.73 10.3409
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001501 4050118 Isolate not provided not provided
Gene Location Start: 2408241;  End: 2408837  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001501_03408.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02869 spore_SleB 1.04e-47 77 198 83 200
spore cortex-lytic enzyme. Members of this protein family are the spore cortex-lytic enzyme SleB from Bacillus subtilis and other Gram-positive, endospore-forming bacterial species. This protein is stored in an inactive form in the spore and activated during germination. [Cellular processes, Sporulation and germination]
COG3773 CwlJ 2.66e-45 67 198 104 242
Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis].
pfam07486 Hydrolase_2 1.32e-44 95 197 1 101
Cell Wall Hydrolase. These enzymes have been implicated in cell wall hydrolysis, most extensively in Bacillus subtilis. For instance Bacillus subtilis steB is expressed during sporulation as an inactive form and then deposited on the cell outer cortex. During germination the the enzyme is activated and hydrolyzes the cortex. A similar role is carried out by the partially redundant Bacillus subtilis CwlJ. It is not clear whether these enzymes are amidases or peptidases.
pfam01476 LysM 3.84e-13 32 74 1 43
LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
PRK06347 PRK06347 2.68e-11 29 82 405 470
1,4-beta-N-acetylmuramoylhydrolase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWI14157.1 6.73e-103 10 198 2 190
AGK55415.1 4.10e-78 1 198 1 199
QGQ46365.1 8.53e-78 1 198 1 200
QIQ32924.1 7.31e-76 21 198 19 197
QNU33833.1 7.31e-76 21 198 19 197

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4F55_A 8.71e-30 68 198 2 128
CrystalStructure of the Catalytic Domain of the Bacillus cereus SleB Protein [Bacillus cereus ATCC 14579]
4FET_A 2.43e-26 73 198 101 222
Catalyticdomain of germination-specific lytic tansglycosylase SleB from Bacillus anthracis [Bacillus anthracis],4FET_B Catalytic domain of germination-specific lytic tansglycosylase SleB from Bacillus anthracis [Bacillus anthracis]
4UZ2_A 7.69e-06 30 75 3 48
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31685 6.97e-36 76 197 90 207
Uncharacterized protein YkvT OS=Bacillus subtilis (strain 168) OX=224308 GN=ykvT PE=2 SV=1
P0A3V1 1.96e-26 73 198 138 259
Spore cortex-lytic enzyme OS=Bacillus cereus OX=1396 GN=sleB PE=1 SV=1
P0A3V0 1.96e-26 73 198 138 259
Spore cortex-lytic enzyme OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=sleB PE=1 SV=1
Q9KCE0 7.17e-25 73 196 209 328
Spore cortex-lytic enzyme OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=sleB PE=3 SV=1
P50739 1.84e-24 73 198 184 305
Spore cortex-lytic enzyme OS=Bacillus subtilis (strain 168) OX=224308 GN=sleB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000559 0.814742 0.183916 0.000259 0.000277 0.000238

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001501_03408.