CAZyme Information: MGYG000002234_01893

Basic Information

• Species: Bariatricus sp900554415
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Bariatricus; Bariatricus sp900554415
• CAZyme ID: MGYG000002234_01893
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1115		127942.06	4.3176

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002234	2915744	MAG	Peru	South America

• Gene Location: Start: 32870; End: 36217 Strand: +

Full Sequence      

MKIQMKRFVAAVLMGVMISSVLPLASVNAAESVEQDNQETVTEESQGLNYVYINKSYVEE
QENQDIMVSWGNEDQNINHMTLQLEDENGKILLLEGKRYEKNTVLFSNLLEKSVYHVTGL
EVTTDTTKYVSMEEYGIQAAFGVGKEYLGEKSDYQSMESIESGAEVGYAVANLNGTDGEE
NAEQVAGVLSNVDISSAVAAMSLSDNEISTQSSTGQLVVVLDPGHDAKHTGARGNGVLEE
VATLKIAQYCKAELQKYNGVEVHLTRDDAACPFPESKDHIDDIKKRVEWAKSIGADVFVS
IHLNSLDGSAAHGAEVYYPSKSSEGKALAQKIQDQLLELGLYDRKIKAEDAYAVVNTSMA
NGFPGLIVEHAFLSNASDASNYLQTEESLQKLGIADATGIARYYGLSKEYWVKIDGKWYY
CNEYGVKQTGWKYINRAWYWLASDGVMQTGWCYINGQWYWFNADGEMQTGWRKLNNQWYW
LTSSGAMQTGWGYIGNQWYWFNSDGEMQSGWLTQGDNKYYLTPSGAGATGWQIIDGKTYY
FDSKCYMLTGTQTIDGTKYEFDRVSGELLKTYIQGWSYENEKWYYYDENENRIVGWSYIN
NEWYWFANDGEMQTDWQYINKKWYWFNNGGAMQTKWGYIDGEWYWFDENGVLQSGWLLLD
GNWFYLQSSGAGAVGWKTIGEKVYYFDSNCYMLTGTQTIDGTKYEFDRVSGELLKTYIQG
WSYENEKWYYYDENENRIVGWSYINNEWYWFANDGEMQTDWQYINKKWYWFNNGGAMQTK
WGYIDGEWYWFDENGVLQSGWLLLDGNWFYLQSSGAGAVGWKTIGEKVYYFDSNCYMLTG
TQIINGTKYEFDRVSGELLKTYIQGWTYENENWYYYDEKGTRIVGWKYINNVWYWFDSNG
VMQTGWKRIDEKWYYFNEDGYWIKQDPVEGIYLIENASGVTVEQMVAYYNSSGREYPEVE
LTMGGAKDITTFCQIYLEEAEAEGIAVEVAFAQAMKETNWLHFGGDVKIEQFNFAGLGAI
GGGVAGMDFSSYGEDGVRMGIRAHIQHLKAYASSEITENTLKNPCVDSRFKYVTKGCAKY
VEWLGQKENPDSYGWATETKYGISIVGMINKMKQF

Enzyme Prediction     

No EC number prediction in MGYG000002234_01893.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	973	1113	4.5e-16	0.9765625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	3.01e-51	218	401	1	172	N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
NF033930	pneumo_PspA	6.22e-46	408	643	442	659	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033930	pneumo_PspA	2.63e-41	613	830	442	635	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
pfam01520	Amidase_3	1.12e-40	219	400	1	172	N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
NF033838	PspC_subgroup_1	1.05e-39	408	643	485	682	pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASM68313.1	2.97e-83	1	423	1	406
QHB24702.1	4.33e-58	929	1113	83	258
QEI32209.1	4.33e-58	929	1113	83	258
QRT30849.1	4.33e-58	929	1113	83	258
CBL26238.1	2.33e-57	923	1113	73	254

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JWQ_A	1.03e-16	218	403	3	175	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5EMI_A	1.96e-16	214	403	2	177	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
3NE8_A	3.28e-11	219	349	7	128	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q02114	2.03e-18	219	404	322	495	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
P54525	4.28e-18	219	404	32	204	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
P50864	1.48e-15	218	404	42	229	Germination-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlD PE=1 SV=1
O48471	3.68e-15	218	409	4	186	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
Q06320	1.70e-14	219	408	4	179	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 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
0.000397	0.998768	0.000206	0.000231	0.000193	0.000164

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002234_01893.