ID A0A377KHH9_9ENTE Unreviewed; 658 AA.
AC A0A377KHH9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN ORFNames=NCTC8129_00758 {ECO:0000313|EMBL:STP28619.1};
OS Enterococcus durans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=53345 {ECO:0000313|EMBL:STP28619.1, ECO:0000313|Proteomes:UP000254070};
RN [1] {ECO:0000313|EMBL:STP28619.1, ECO:0000313|Proteomes:UP000254070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC8129 {ECO:0000313|EMBL:STP28619.1,
RC ECO:0000313|Proteomes:UP000254070};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC {ECO:0000256|ARBA:ARBA00010266}.
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DR EMBL; UGIF01000002; STP28619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377KHH9; -.
DR Proteomes; UP000254070; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Glycosidase {ECO:0000313|EMBL:STP28619.1};
KW Hydrolase {ECO:0000313|EMBL:STP28619.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 250..293
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 328..371
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 402..445
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 476..519
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 556..599
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 613..656
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 224..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 70195 MW; 9F1BDDEA8512B552 CRC64;
MENIARKERR RLEETKRFRK VKRSAALVGT AMVGCSVAAP LIQPVPVNAD QTPTQFGARI
NTAAFITEIA TYAQPIAQAN DLYASVMIAQ AVVESGWGSS ALSQAPYHNL FGIKGSYQGQ
TVYMDTLEYL NNQWVTKKEP FRQYPSFAES FSDNAYVLRN TSFGNGHYYA GTWKSNTKSY
TDATAYLTGR YATDPSYAGK LNNIILTYGL TKYDTPASGN AGGGATTGGN TNTGNTGSNA
NTGSTGTTST TYTVKSGDSV WGISNSFGIS MSQLIEWNNI KNNFIYPGQK LTIKGGQTTG
SSTNNSGNNT NSSGNSNTSA GTGQTSGAKY TVKSGDSVWK IANDHGISMN QLIQWNNIKN
NFVYPGQQLI VSNGGSSSST TTNTGNASSS SNNAGNTAVS GTKYTVKSGD SVWSVSNKYG
ISMNQLIQWN NIKNNFIYPG QQLVVSNGSS SSSATTNQNT TNNTNTNTGA TTNTGSTYTV
KAGESVWSVA NKNGISMDQL IQWNNIKNNF IYPGQQLIVK GGSAATSTNT SSTTAATTPS
TPNTSNTTST ASTGDTIYTV KAGESVWGVA NKHNITMDQL IQWNNIKNNF IYPGQQVIVK
KGTTQSAPTT GQKTYTVKAG ESVWGVADSH GITMNQLIEW NNIKNNFIYP GQQLIVAK
//
