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Database: UniProt
Entry: E7GQH9_CLOSY
LinkDB: E7GQH9_CLOSY
Original site: E7GQH9_CLOSY 
ID   E7GQH9_CLOSY            Unreviewed;       600 AA.
AC   E7GQH9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Muramidase {ECO:0000313|EMBL:EGA93026.1};
GN   ORFNames=HMPREF9474_03174 {ECO:0000313|EMBL:EGA93026.1};
OS   [Clostridium] symbiosum WAL-14163.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=742740 {ECO:0000313|EMBL:EGA93026.1, ECO:0000313|Proteomes:UP000002970};
RN   [1] {ECO:0000313|EMBL:EGA93026.1, ECO:0000313|Proteomes:UP000002970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL-14163 {ECO:0000313|EMBL:EGA93026.1,
RC   ECO:0000313|Proteomes:UP000002970};
RA   Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA   Molitoris D.R., Vaisanen M.L., Daigneault M., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA   Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium symbiosum strain WAL-14163.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endohydrolysis of the di-N-acetylchitobiosyl unit in high-
CC       mannose glycopeptides and glycoproteins containing the
CC       -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue
CC       remains attached to the protein; the rest of the oligosaccharide is
CC       released intact. Cleaves the peptidoglycan connecting the daughter
CC       cells at the end of the cell division cycle, resulting in the
CC       separation of the two newly divided cells. Acts as an autolysin in
CC       penicillin-induced lysis. {ECO:0000256|ARBA:ARBA00043889}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGA93026.1}.
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DR   EMBL; ADLQ01000071; EGA93026.1; -; Genomic_DNA.
DR   RefSeq; WP_003502324.1; NZ_GL834313.1.
DR   AlphaFoldDB; E7GQH9; -.
DR   STRING; 1512.GCA_900049235_03430; -.
DR   eggNOG; COG1705; Bacteria.
DR   eggNOG; COG5632; Bacteria.
DR   HOGENOM; CLU_042024_3_0_9; -.
DR   Proteomes; UP000002970; Unassembled WGS sequence.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   SMART; SM00047; LYZ2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002970}.
FT   DOMAIN          3..164
FT                   /note="Mannosyl-glycoprotein endo-beta-N-
FT                   acetylglucosamidase-like"
FT                   /evidence="ECO:0000259|SMART:SM00047"
FT   REGION          372..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   600 AA;  66627 MW;  CC5C2E1BC31AADAD CRC64;
     MKEQDFIQKI CGYAISDMKE NGILASVTIA QAILESSWGT SELAKKANNY FGMKCSLSSN
     SWGSVWDRVS KYTKVTNEQD EAGKIYTIKA DFRAYPDIEM SIKDHSMYLV GAMNGTEHRY
     CGIANEKDYR KAVEIIKAGG YATDINYVSK ICSIIKKYEL TQYDEMEELN MGIEIRKQIA
     TNSPCNKTGD EITVKGSMLH SVGCPQPKPE VFAKIWETST GACVHAVTGA DAYAIQCLPL
     FPERKKARRG WHGASGKNGS VNNTHLSLEM TEPATIKYVG GATWIETGDG SNTKRHVLAT
     YANAVKLFAE WCSEFGLNPL EDGVIISHHE GNQRGIASNH GDVEHIWNKF GLTMNQFRQD
     VNKAMRGQVV DTVPTTPVDN SSDDKSSQSV NPLSGTVTVI YEGDDGLNVR KAPSITADVD
     QIVYNGVYTV VGISADEKWY KLKSGLFITT IPEYVSFKAT PEQKQQTAGT GYYRVRKSWN
     DAGSQIGAFK NQNNAIELCK QNSGYKVFDN DGNEIYPCIK DDGTPFKFRV TIPDLRIRKG
     PGTTYDYWKK NGSPEYTGKN VFTIIDTAEG PGAKIWGLLK SGEKDRDRWI SLDEDYGNRL
//
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