CAZyme Information: MGYG000004223_00442

Basic Information

• Species: UMGS1883 sp900763305
• Lineage: Bacteria; Firmicutes_A; Clostridia; UMGS1883; UMGS1883; UMGS1883; UMGS1883 sp900763305
• CAZyme ID: MGYG000004223_00442
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
282	MGYG000004223_3|CGC3	30163.52	5.3805

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004223	2575981	MAG	United Kingdom	Europe

• Gene Location: Start: 94012; End: 94860 Strand: -

Full Sequence      

MNGCAVFYTVEEGNTILSIAELFGTSPESILRLNPSVDPDNLEIGTRLCVVSATVQPVQC
PPGSIAYNINRGDTLGTIAERFGTTAENILLTNPTLDPYNLRIGQRICIEQPIPELPDCK
TRNFYVIRSGDTLGAIAASFGVKASEIRAANPGINPNNLTVGSVICIPLAPSPIDVIINV
AAKRLTVYKKGSIYREYIIATGKPETPTPIGNFTIINKELDPGGPYGTRWLGLSKRGYGI
HGTNNPPSIGTAASNGCIRMYNEDAEALFDMTPVGTSVRILP

Enzyme Prediction     

No EC number prediction in MGYG000004223_00442.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16913	YkuD_like	6.91e-42	176	280	2	120	L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD. Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.
COG1376	ErfK	3.05e-25	147	280	60	228	Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis].
pfam03734	YkuD	4.62e-23	176	280	4	89	L,D-transpeptidase catalytic domain. This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.
PRK10260	PRK10260	1.20e-13	104	281	33	234	L,D-transpeptidase; Provisional
smart00257	LysM	6.54e-13	124	167	1	44	Lysin motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALX07568.1	3.92e-104	6	280	14	288
ANV75308.1	3.92e-104	6	280	14	288
ADU73640.1	3.92e-104	6	280	14	288
ABN54202.1	7.88e-104	6	280	14	288
AOT72145.1	3.23e-93	6	280	15	288

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2MTZ_A	1.45e-40	125	280	7	165	Haddockmodel of Bacillus subtilis L,D-transpeptidase in complex with a peptidoglycan hexamuropeptide [Bacillus subtilis],3ZQD_A B. subtilis L,D-transpeptidase [Bacillus subtilis subsp. subtilis str. 168],4A52_A NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
4A1I_A	1.69e-39	125	280	5	163	ykudfrom B.subtilis [Bacillus subtilis],4A1I_B ykud from B.subtilis [Bacillus subtilis],4A1I_C ykud from B.subtilis [Bacillus subtilis],4A1I_D ykud from B.subtilis [Bacillus subtilis],4A1I_E ykud from B.subtilis [Bacillus subtilis],4A1I_F ykud from B.subtilis [Bacillus subtilis],4A1I_G ykud from B.subtilis [Bacillus subtilis],4A1I_H ykud from B.subtilis [Bacillus subtilis],4A1J_A Ykud L,D-transpeptidase from B.subtilis [Bacillus subtilis],4A1J_B Ykud L,D-transpeptidase from B.subtilis [Bacillus subtilis]
1Y7M_A	1.29e-38	125	280	4	162	ChainA, Crystal Structure of the B. subtilis YkuD protein at 2 A resolution [Bacillus subtilis subsp. subtilis str. 168],1Y7M_B Chain B, Crystal Structure of the B. subtilis YkuD protein at 2 A resolution [Bacillus subtilis subsp. subtilis str. 168]
4A1K_A	5.25e-38	125	280	5	163	YkudL,D-transpeptidase [Bacillus subtilis]
4B8V_A	2.40e-17	8	168	44	217	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q5WC42	3.77e-47	124	282	3	165	Putative L,D-transpeptidase YkuD OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=ABC3535 PE=3 SV=1
O34816	5.72e-40	125	280	4	162	Putative L,D-transpeptidase YkuD OS=Bacillus subtilis (strain 168) OX=224308 GN=ykuD PE=1 SV=1
Q65K99	9.25e-39	125	282	4	165	Putative L,D-transpeptidase YkuD OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi01617 PE=3 SV=1
P54539	1.74e-18	168	280	17	150	Putative L,D-transpeptidase YqjB OS=Bacillus subtilis (strain 168) OX=224308 GN=yqjB PE=3 SV=1
P40680	5.18e-11	133	281	50	231	Probable L,D-transpeptidase ErfK/SrfK OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=erfK PE=3 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
1.000050	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004223_00442.