ID A0A2S4ZZW9_9SPHI Unreviewed; 288 AA.
AC A0A2S4ZZW9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN ORFNames=C3K47_14530 {ECO:0000313|EMBL:POY35609.1};
OS Solitalea longa.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Solitalea.
OX NCBI_TaxID=2079460 {ECO:0000313|EMBL:POY35609.1, ECO:0000313|Proteomes:UP000236893};
RN [1] {ECO:0000313|EMBL:POY35609.1, ECO:0000313|Proteomes:UP000236893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-AV {ECO:0000313|EMBL:POY35609.1,
RC ECO:0000313|Proteomes:UP000236893};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:POY35609.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PQVF01000010; POY35609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4ZZW9; -.
DR OrthoDB; 977752at2; -.
DR Proteomes; UP000236893; Unassembled WGS sequence.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022638};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000236893};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..288
FT /note="Peptidoglycan hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015596166"
FT DOMAIN 243..286
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 32003 MW; 0F6AB169559DB2C8 CRC64;
MNSWKTLTLC IIAYSFVACS AKKNVTLPNN SSQSISASNS GNKKAPATTT YAKSSSTQQY
INKYKQVAID EMHRTGIPAS ITLAQAIFES SSGNSDLATS ANNHFGIKCT SDWQGPTYHK
DDDRPNECFR KYPHAEGSFR DHSEFLKRPR YAGLFKLERT DYQGWANGLK TAGYATNPQY
GPKLIEVIER YELYKFDKSA SKDPVASSGD RGSLYFEQKP VNEEGKIASK STQSDNEEVV
PAGFYRVKAG DTLYGIAKKF NTKVENIVTW NNLESYSIAV GQLLKISK
//
