ID A0A0U3PRC3_9LACT Unreviewed; 1276 AA.
AC A0A0U3PRC3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN ORFNames=NY10_2279 {ECO:0000313|EMBL:ALV22864.1};
OS Carnobacterium sp. CP1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV22864.1, ECO:0000313|Proteomes:UP000064734};
RN [1] {ECO:0000313|EMBL:ALV22864.1, ECO:0000313|Proteomes:UP000064734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP1 {ECO:0000313|EMBL:ALV22864.1,
RC ECO:0000313|Proteomes:UP000064734};
RA Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT Amanda bay, East Antarctic.";
RL Submitted (FEB-2015) 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; CP010796; ALV22864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3PRC3; -.
DR STRING; 1564681.NY10_2279; -.
DR KEGG; carc:NY10_2279; -.
DR PATRIC; fig|1564681.3.peg.2288; -.
DR Proteomes; UP000064734; Chromosome.
DR GO; GO:0005576; C:extracellular region; 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; 11.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 11.
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; 11.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00257; LysM; 11.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF54106; LysM domain; 11.
DR PROSITE; PS51782; LYSM; 11.
PE 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Reference proteome {ECO:0000313|Proteomes:UP000064734};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 379..422
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 632..675
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 699..742
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 766..809
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 833..876
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 898..941
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 965..1008
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 1032..1075
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 1097..1140
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 1172..1215
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 1232..1275
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 64..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 133939 MW; 40A0B766E735D65D CRC64;
MEKTRKERIV AANSKKLFGK KDLSNAVYKR GTAVLSTTLL VSLLAFPSFS ASASANDLAN
SSSKELEENL KNNPEVVTEG TTEGTEVAKE SETSIQSTEK SSDTTENAAE DKAIEKEQKI
QELKILLTAE VFDTLIFEEL DMEDIDELIE TALDVKNDDT VNSEEAIEAT ITKMSIATNE
EKIEATYALT EETVETDAVV EETSAAVNEG IEPSESAVEA EASLTTEIVE KSEEVSDVDK
AAEQAELDKA EADKVKADQA AADKAELDQA ASEQAELEQA AADKAKAEQA AADKAKTDQA
AADKAKAEQA ADKAKAEQAA DKAKAEQAAA DKAKADKAAA DKAKADKAAA DKAKADKAAA
DKAKADKAAA DKAKAETAKL YTIKSGDTLN KIAKANGLSV AELKKMNNLS SDLIHPGQVL
AVNKAAVGAV QTVTTAITSN KAIEKMSNAE FVEFIGAYAA EVAPKNDLYA SLMIAQAALE
SGWGSSKLSS SPNHNLFGIK GSYNGQTATM YTSEWSASGG WIYIPQNFKK YPSHAESLQD
NANLLKNGTN WDSNFYSGAW KSNSTSVYDA TAWLQGRYAT DPSYASKLNN IINSYNLTRF
DSGYTGPVNP NPGSTGSDSS SSEKPNTNTT ASSYTVKNGD TLWAIANRMG VSVANVKSWN
NLKSDTIYIG QKLTIKGGTG STNNNSTPNT STPSNTTTSS YTVKSGDTLW GVASSKGVSV
ANLKSWNNLT SDTIYIDQKL TIKGGTGSTN NNSTPNTSTP SNTATSSYTV KSGDTLWGVA
NSSGVSVANL KSWNNLTSDT IYIGQKLTIK GGTGSTNNNS TPNTSTPSNT ATSTYTVKNG
DTLWGVANSK GVSVANLKSW NNLTSDTIFV GQNLTIKGGT GSTNTTPTTS TPTNTATSTY
TVKSGDTLWE VASSNGVSVA NLKSWNNLTS DTIFVGQKLT IKGGTNSSSA NTAPNISTPS
NTVTSSYTVK NGDSLWGVAS SNGVSVANLK SWNNLTSDTI YIGQNLTIKG GTGSTNNNST
PNTSTPSNTT TSSYTVKSGD TLWGVASSKG VSVANLKSWN NLTSDTIMVG QNLTIKGGST
ATTNSNKTDA TVSNLAVSYT IKSGDTLSAI SSKYGVSLSD LKSWNKLSTD TIYVGQTLTV
KVGNQANSIA TAKTPTVPVP TTNKNTSGAA QSNHIVKSGD TLWGIANSNG VSVADLKSWN
DLNSDSLSVG QNLTLITSVK SDVVTKTPEQ LASYTVVRDD SLWAIANKIG VSVASLKEWN
YLKSDVIFVG QTLLIK
//
