CWLM_MYCTU
ID CWLM_MYCTU Reviewed; 406 AA.
AC L7N653; I6YHG7;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase CwlM {ECO:0000305|PubMed:15680239};
DE EC=3.5.1.28 {ECO:0000269|PubMed:15680239};
DE AltName: Full=Peptidoglycan hydrolase CwlM {ECO:0000303|PubMed:15680239};
GN Name=cwlM {ECO:0000303|PubMed:15680239};
GN OrderedLocusNames=Rv3915 {ECO:0000312|EMBL:CCP46744.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RC STRAIN=BMC 2732386;
RX PubMed=15680239; DOI=10.1016/j.bbapap.2004.09.021;
RA Deng L.L., Humphries D.E., Arbeit R.D., Carlton L.E., Smole S.C.,
RA Carroll J.D.;
RT "Identification of a novel peptidoglycan hydrolase CwlM in Mycobacterium
RT tuberculosis.";
RL Biochim. Biophys. Acta 1747:57-66(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Cell-wall hydrolase that hydrolyzes the amide bond between N-
CC acetylmuramic acid and L-alanine in cell-wall glycopeptides. Is able to
CC lyse whole mycobacteria, release peptidoglycan from the cell wall of
CC M.luteus and M.smegmatis, and cleave N-acetylmuramoyl-L-alanyl-D-
CC isoglutamine, releasing free N-acetylmuramic acid and dipeptide.
CC {ECO:0000269|PubMed:15680239}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000269|PubMed:15680239};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. Activity is greater than 50% of maximal from pH
CC 6.2 to 9.2. Is stable throughout a broad range of pH (6-10).
CC {ECO:0000269|PubMed:15680239};
CC -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC {ECO:0000269|PubMed:15680239}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:15680239}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46744.1; -; Genomic_DNA.
DR RefSeq; WP_003400168.1; NZ_NVQJ01000005.1.
DR RefSeq; YP_178027.1; NC_000962.3.
DR AlphaFoldDB; L7N653; -.
DR SMR; L7N653; -.
DR STRING; 83332.Rv3915; -.
DR PaxDb; L7N653; -.
DR PRIDE; L7N653; -.
DR DNASU; 886250; -.
DR GeneID; 886250; -.
DR KEGG; mtu:Rv3915; -.
DR PATRIC; fig|83332.111.peg.4360; -.
DR TubercuList; Rv3915; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG3409; Bacteria.
DR OMA; GVATYHY; -.
DR PhylomeDB; L7N653; -.
DR UniPathway; UPA00549; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 1.10.101.10; -; 2.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF01471; PG_binding_1; 2.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF47090; SSF47090; 2.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Hydrolase; Periplasm; Reference proteome;
KW Repeat.
FT CHAIN 1..406
FT /note="N-acetylmuramoyl-L-alanine amidase CwlM"
FT /id="PRO_0000434795"
FT DOMAIN 193..370
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000255"
FT REGION 18..83
FT /note="Peptidoglycan-binding domain 1"
FT /evidence="ECO:0000305|PubMed:15680239"
FT REGION 105..160
FT /note="Peptidoglycan-binding domain 2"
FT /evidence="ECO:0000305|PubMed:15680239"
SQ SEQUENCE 406 AA; 43912 MW; 8D58901676B47213 CRC64;
MPSPRREDGD ALRCGDRSAA VTEIRAALTA LGMLDHQEED LTTGRNVALE LFDAQLDQAV
RAFQQHRGLL VDGIVGEATY RALKEASYRL GARTLYHQFG APLYGDDVAT LQARLQDLGF
YTGLVDGHFG LQTHNALMSY QREYGLAADG ICGPETLRSL YFLSSRVSGG SPHAIREEEL
VRSSGPKLSG KRIIIDPGRG GVDHGLIAQG PAGPISEADL LWDLASRLEG RMAAIGMETH
LSRPTNRSPS DAERAATANA VGADLMISLR CETQTSLAAN GVASFHFGNS HGSVSTIGRN
LADFIQREVV ARTGLRDCRV HGRTWDLLRL TRMPTVQVDI GYITNPHDRG MLVSTQTRDA
IAEGILAAVK RLYLLGKNDR PTGTFTFAEL LAHELSVERA GRLGGS
