MUR2_ENTHA
ID MUR2_ENTHA Reviewed; 666 AA.
AC P39046; I6TA70;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Muramidase-2;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramoylhydrolase;
DE AltName: Full=Lysozyme;
DE AltName: Full=Peptidoglycan hydrolase;
DE AltName: Full=Pg-hydrolase 2;
DE Flags: Precursor;
GN OrderedLocusNames=EHR_05900;
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 50-73.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=1347040; DOI=10.1128/jb.174.5.1619-1625.1992;
RA Chu C.-P., Kariyama R., Daneo-Moore L., Shockman G.D.;
RT "Cloning and sequence analysis of the muramidase-2 gene from Enterococcus
RT hirae.";
RL J. Bacteriol. 174:1619-1625(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=22933757; DOI=10.1128/jb.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=2753858; DOI=10.1128/jb.171.8.4355-4361.1989;
RA Dolinger D.L., Daneo-Moore L., Shockman G.D.;
RT "The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790
RT covalently binds penicillin.";
RL J. Bacteriol. 171:4355-4361(1989).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RA Del Mar Lleo M., Canepari P., Satta G.;
RT "Thermosensitive cell growth mutants of Enterococcus hirae that elongate at
RT non-permissive temperature are stimulated to divide by parental autolytic
RT enzymes.";
RL J. Gen. Microbiol. 139:3099-3117(1993).
CC -!- FUNCTION: May work in concert with and potentiate the processive
CC hydrolytic action of muramidase-1, which requires binding of the enzyme
CC to non-reducing ends of glycan chains. Hydrolysis in the midst of
CC glycan chains would increase the number of binding sites for
CC muramidase-1. May function in facilitating septum formation and cell
CC separation. Active on M.luteus cell walls and on E.hirae cell wall
CC fractions, but not active on E.hirae intact cell walls. Can covalently
CC bind penicillin. {ECO:0000269|PubMed:2753858, ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC binding.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family. {ECO:0000305}.
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DR EMBL; M77639; AAA24776.1; -; Genomic_DNA.
DR EMBL; CP003504; AFM70129.1; -; Genomic_DNA.
DR PIR; A42296; A42296.
DR RefSeq; WP_010736969.1; NZ_KB946228.1.
DR AlphaFoldDB; P39046; -.
DR SMR; P39046; -.
DR STRING; 768486.EHR_05900; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR PRIDE; P39046; -.
DR EnsemblBacteria; AFM70129; AFM70129; EHR_05900.
DR KEGG; ehr:EHR_05900; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG1705; Bacteria.
DR HOGENOM; CLU_013771_6_1_9; -.
DR OrthoDB; 682655at2; -.
DR Proteomes; UP000002895; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 6.
DR Gene3D; 3.10.350.10; -; 6.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF01476; LysM; 6.
DR SMART; SM00257; LysM; 6.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF54106; SSF54106; 6.
DR PROSITE; PS51782; LYSM; 6.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Cell cycle; Cell division;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Glycosidase;
KW Hydrolase; Repeat; Secreted; Septation; Signal.
FT SIGNAL 1..49
FT /evidence="ECO:0000269|PubMed:1347040"
FT CHAIN 50..666
FT /note="Muramidase-2"
FT /id="PRO_0000012120"
FT DOMAIN 255..298
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 336..379
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 412..455
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 487..530
FT /note="LysM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 563..606
FT /note="LysM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 621..664
FT /note="LysM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 232..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 70670 MW; FF0A7FAFCD810BA3 CRC64;
MENIARKERR RLNETKRFRK VKRSAALVGT AMVGCSVAAP LIQPVQVDAD QTPTQFGARI
NTAAFIAEIA TYAQPIAQAN DLYASVMIAQ AVVESGWGSS ALSQAPYYNL FGIKGSYQGQ
TVYMDTLEYL NNKWVSKKEP FRQYPSFAES FNDNAYVLRN TSFGNGYYYA GTWKSNTKSY
TDATACLTGR YATDPGYAGK LNNIITTYGL TKYDTPASGN AGGGVTIGNG GNTGNTSNSG
STSGNSGGSA TTTGTTYTVK SGDSVWGISH SFGITMAQLI EWNNIKNNFI YPGQKLTIKG
GQSAGSSTTN TGNNASSGNT SGNTNTSGST GQATGAKYTV KSGDSVWKIA NDHGISMNQL
IEWNNIKNNF VYPGQQLVVS KGSSSASGST SNTSTGNTSS NTANTGSTTS GSTYTVKAGE
SVWSVSNKFG ISMNQLIQWN NIKNNFIYPG QKLIVKGGSS SSNASTSTAN NKNTASSNTS
STATGQATYT VKAGESVWGV ANKNGISMNQ LIEWNNIKNN FIYPGQKLIV KGGSSKASAT
ATIKPTASTP ASTTPTASST GDTKYTVKAG ESVWGVANKH HITMDQLIEW NNIKNNFIYP
GQEVIVKKGT AQSTPAKSDE KTYTVKAGES VWGVADSHGI TMNQLIEWNN IKNNFIYPGQ
QLIVKK
