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   27-MAR-2024, entry version 132.
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; Bacillota; 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
RC   6459 / 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
RC   6459 / 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
RC   6459 / 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
RC   6459 / 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   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   KEGG; ehr:EHR_05900; -.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG1705; Bacteria.
DR   HOGENOM; CLU_013771_6_1_9; -.
DR   OrthoDB; 2155627at2; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 6.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 6.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   PANTHER; PTHR33734:SF35; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 1; 1.
DR   PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF01476; LysM; 6.
DR   SMART; SM00257; LysM; 6.
DR   SMART; SM00047; LYZ2; 1.
DR   SUPFAM; SSF54106; LysM domain; 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; Reference proteome; 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
//