PEPAM_MYCTU
ID PEPAM_MYCTU Reviewed; 241 AA.
AC I6Y4D2;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase Rv3717 {ECO:0000303|PubMed:24019530, ECO:0000303|PubMed:24311595};
DE EC=3.5.1.28 {ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595};
DE AltName: Full=Zinc-dependent peptidoglycan amidase {ECO:0000303|PubMed:24019530};
DE Flags: Precursor;
GN OrderedLocusNames=Rv3717 {ECO:0000312|EMBL:CCP46543.1};
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 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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 25-241 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY
RP REGULATION, SUBUNIT, AND PATHWAY.
RC STRAIN=H37Rv;
RX PubMed=24311595; DOI=10.1107/s0907444913026371;
RA Kumar A., Kumar S., Kumar D., Mishra A., Dewangan R.P., Shrivastava P.,
RA Ramachandran S., Taneja B.;
RT "The structure of Rv3717 reveals a novel amidase from Mycobacterium
RT tuberculosis.";
RL Acta Crystallogr. D 69:2543-2554(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-241 OF APOENZYME AND IN
RP COMPLEXES WITH ZINC AND THE DIPEPTIDE PRODUCT L-ALANINE-ISO-D-GLUTAMINE,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISULFIDE BOND, MUTAGENESIS OF
RP GLU-200, ACTIVE SITE, AND PATHWAY.
RX PubMed=24019530; DOI=10.1074/jbc.m113.510792;
RA Prigozhin D.M., Mavrici D., Huizar J.P., Vansell H.J., Alber T.;
RT "Structural and biochemical analyses of Mycobacterium tuberculosis N-
RT acetylmuramyl-L-alanine amidase Rv3717 point to a role in peptidoglycan
RT fragment recycling.";
RL J. Biol. Chem. 288:31549-31555(2013).
CC -!- FUNCTION: Cell-wall hydrolase that hydrolyzes the amide bond between N-
CC acetylmuramic acid and L-alanine in cell-wall glycopeptides
CC (PubMed:24311595, PubMed:24019530). Is able to hydrolyze the cell walls
CC of several bacterial species (i.e. Paenibacillus sp., B.avium, E.coli
CC DH5alpha, E.aerogenes, L.acidophilus, B.thuringiensis, B.pumilus,
CC B.subtilis and E.coli W3110), thereby showing that it is a cell-wall
CC hydrolase with broad-spectrum activity (PubMed:24311595). May have a
CC role in peptidoglycan fragment recycling (PubMed:24019530).
CC {ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595}.
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:24019530, ECO:0000269|PubMed:24311595};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595};
CC -!- ACTIVITY REGULATION: The structure reveals a short flexible hairpin
CC turn that partially occludes the active site and may be involved in
CC autoregulation. {ECO:0000305|PubMed:24311595}.
CC -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC {ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24311595}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:24019530}.
CC -!- MISCELLANEOUS: Disulfide oxidation is not required for folding of the
CC enzyme core or in vitro muramyl dipeptide hydrolysis.
CC {ECO:0000269|PubMed:24019530}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP46543.1; -; Genomic_DNA.
DR RefSeq; NP_218234.1; NC_000962.3.
DR RefSeq; WP_003420410.1; NC_000962.3.
DR PDB; 4LQ6; X-ray; 1.68 A; A=25-241.
DR PDB; 4M6G; X-ray; 2.10 A; A=20-241.
DR PDB; 4M6H; X-ray; 2.19 A; A/B=20-241.
DR PDB; 4M6I; X-ray; 2.67 A; A/B=20-241.
DR PDBsum; 4LQ6; -.
DR PDBsum; 4M6G; -.
DR PDBsum; 4M6H; -.
DR PDBsum; 4M6I; -.
DR AlphaFoldDB; I6Y4D2; -.
DR SMR; I6Y4D2; -.
DR STRING; 83332.Rv3717; -.
DR PaxDb; I6Y4D2; -.
DR DNASU; 885602; -.
DR GeneID; 885602; -.
DR KEGG; mtu:Rv3717; -.
DR PATRIC; fig|83332.111.peg.4133; -.
DR TubercuList; Rv3717; -.
DR eggNOG; COG0860; Bacteria.
DR OMA; RIMRDQM; -.
DR PhylomeDB; I6Y4D2; -.
DR BRENDA; 3.5.1.28; 3445.
DR UniPathway; UPA00549; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
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 InterPro; IPR002508; MurNAc-LAA_cat.
DR Pfam; PF01520; Amidase_3; 1.
DR SMART; SM00646; Ami_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Disulfide bond; Hydrolase;
KW Metal-binding; Periplasm; Reference proteome; Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..241
FT /note="N-acetylmuramoyl-L-alanine amidase Rv3717"
FT /id="PRO_5004159884"
FT DOMAIN 29..230
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000255"
FT REGION 45..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:24019530"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24019530,
FT ECO:0000269|PubMed:24311595, ECO:0007744|PDB:4LQ6,
FT ECO:0007744|PDB:4M6G, ECO:0007744|PDB:4M6I"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24019530,
FT ECO:0000269|PubMed:24311595, ECO:0007744|PDB:4LQ6,
FT ECO:0007744|PDB:4M6G, ECO:0007744|PDB:4M6I"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24019530,
FT ECO:0000269|PubMed:24311595, ECO:0007744|PDB:4LQ6,
FT ECO:0007744|PDB:4M6G, ECO:0007744|PDB:4M6I"
FT DISULFID 57..105
FT /evidence="ECO:0000269|PubMed:24019530"
FT MUTAGEN 200
FT /note="E->A,Q: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24019530"
SQ SEQUENCE 241 AA; 24836 MW; 719D0F523A4B9C0C CRC64;
MIVGVLVAAA TPIISSASAT PANIAGMVVF IDPGHNGAND ASIGRQVPTG RGGTKNCQAS
GTSTNSGYPE HTFTWETGLR LRAALNALGV RTALSRGNDN ALGPCVDERA NMANALRPNA
IVSLHADGGP ASGRGFHVNY SAPPLNAIQA GPSVQFARIM RDQLQASGIP KANYIGQDGL
YGRSDLAGLN LAQYPSILVE LGNMKNPADS ALMESAEGRQ KYANALVRGV AGFLATQGQA
R
