ID R2STL9_9ENTE Unreviewed; 285 AA.
AC R2STL9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN ORFNames=UAW_01176 {ECO:0000313|EMBL:EOH98580.1};
OS Enterococcus haemoperoxidus ATCC BAA-382.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH98580.1, ECO:0000313|Proteomes:UP000013858};
RN [1] {ECO:0000313|EMBL:EOH98580.1, ECO:0000313|Proteomes:UP000013858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH98580.1,
RC ECO:0000313|Proteomes:UP000013858};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus haemoperoxidus BAA-382.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC {ECO:0000256|ARBA:ARBA00010266}.
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:EOH98580.1}.
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DR EMBL; AJAR01000012; EOH98580.1; -; Genomic_DNA.
DR RefSeq; WP_010761384.1; NZ_KE136479.1.
DR AlphaFoldDB; R2STL9; -.
DR STRING; 155618.RV06_GL001263; -.
DR PATRIC; fig|1158608.3.peg.1150; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG1705; Bacteria.
DR OrthoDB; 2155627at2; -.
DR Proteomes; UP000013858; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; 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; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
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; PF01832; Glucosaminidase; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..284
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 30313 MW; 0D834356E245BF6B CRC64;
MDEIKTRSSR HQQQNLKKNR KRVASVIGTS LVFLPIAGNL LPLGVQATEV ETQGAISQQA
FIDSIGYSAA SVADVNDLYA SVMIAQALLE SSYGTSGLAA APNYNLFGVK GSYGGQSVYM
PTSEYLNGEW VTVTEPFRSY PSYAESFQDH ANVLKTTLAS SGNYHYSGVW KSNTSSYMDA
TAALAGRYAT DPNYASKLNW LIEAYGLTAY DSGITQSTVT SDNAASTQST IGQSSATNTV
STYTVASGDT LWGISEKFGI SVDQLMASNG ITAELITVGQ VLQIA
//