CAZyme Information: MGYG000002252_00289

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; UMGS1883; UMGS1883; UMGS1883
• CAZyme ID: MGYG000002252_00289
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
281		30520.03	5.0786

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002252	1068646	MAG	Peru	South America

• Gene Location: Start: 3006; End: 3851 Strand: +

Full Sequence      

MACALYYTIQEGDILSNIANRFNTTVENLLRLNERLDPDNLPIGEDICIVSKTVQPVSCP
YGSLPYNIKPGDTLASIASEFDTTPDALILLNPDIDPYNLQVGSRICIAQRFTPPPDCPT
KNYYVIRRGDTLSAIAGIFGVTVREILRINPGLNPNNLTIGQIICIPAAPSPIEIIINVA
AKRLTVYRKGIIYREYIVATGRPETPTPLGNFTVVNKETDPGGPYGTRWMGLSKAGYGIH
GTNNPASIGTAASNGCIRMYNEDVEALFDITPVGTPVRILP

Enzyme Prediction     

No EC number prediction in MGYG000002252_00289.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16913	YkuD_like	1.10e-41	175	279	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	1.86e-24	155	279	74	228	Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis].
pfam03734	YkuD	5.71e-23	175	279	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.
smart00257	LysM	1.88e-14	123	166	1	44	Lysin motif.
smart00257	LysM	3.85e-13	6	49	1	44	Lysin motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALX07568.1	2.07e-113	7	279	16	288
ANV75308.1	2.07e-113	7	279	16	288
ADU73640.1	2.07e-113	7	279	16	288
ABN54202.1	1.19e-112	7	279	16	288
AOT72145.1	5.42e-99	7	279	17	288

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2MTZ_A	8.97e-42	124	279	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	9.40e-42	124	279	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	7.20e-41	124	279	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	2.94e-40	124	279	5	163	YkudL,D-transpeptidase [Bacillus subtilis]
4B8V_A	3.37e-18	7	167	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	4.59e-48	123	281	3	165	Putative L,D-transpeptidase YkuD OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=ABC3535 PE=3 SV=1
O34816	3.54e-41	124	279	4	162	Putative L,D-transpeptidase YkuD OS=Bacillus subtilis (strain 168) OX=224308 GN=ykuD PE=1 SV=1
Q65K99	7.26e-41	124	281	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	1.23e-17	170	279	24	150	Putative L,D-transpeptidase YqjB OS=Bacillus subtilis (strain 168) OX=224308 GN=yqjB PE=3 SV=1
Q49UX4	1.90e-10	4	162	26	189	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 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
1.000031	0.000006	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002252_00289.