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Database: UniProt
Entry: A0A0Q1HCB6_9FLAO
LinkDB: A0A0Q1HCB6_9FLAO
Original site: A0A0Q1HCB6_9FLAO 
ID   A0A0Q1HCB6_9FLAO        Unreviewed;       284 AA.
AC   A0A0Q1HCB6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN   ORFNames=AAY42_15465 {ECO:0000313|EMBL:KQC31134.1};
OS   Allomuricauda eckloniae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=346185 {ECO:0000313|EMBL:KQC31134.1, ECO:0000313|Proteomes:UP000050827};
RN   [1] {ECO:0000313|EMBL:KQC31134.1, ECO:0000313|Proteomes:UP000050827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK169 {ECO:0000313|EMBL:KQC31134.1,
RC   ECO:0000313|Proteomes:UP000050827};
RA   Kwon Y.M., Kim S.-J.;
RT   "Complete genome of flavobacterium.";
RL   Submitted (APR-2015) 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:KQC31134.1}.
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DR   EMBL; LCTZ01000002; KQC31134.1; -; Genomic_DNA.
DR   RefSeq; WP_055396829.1; NZ_LCTZ01000002.1.
DR   AlphaFoldDB; A0A0Q1HCB6; -.
DR   STRING; 346185.AAY42_15465; -.
DR   PATRIC; fig|1547436.3.peg.3190; -.
DR   OrthoDB; 977752at2; -.
DR   Proteomes; UP000050827; 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:UP000050827};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..284
FT                   /note="Peptidoglycan hydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006190500"
FT   DOMAIN          234..277
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          29..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   284 AA;  32680 MW;  16A4AE5ADEAC7535 CRC64;
     MIRRIGCIVV LTLMLVSCGA KKRTVTKEQK AVTEARKHRN PNAGIPTDGP KESELYPLPV
     NPGRFVKFPI ANTQEYIETF AQMAQYEMRA FGIPASITLA QGILESGSGK GELTQKTNNH
     FGIKCHTGWD GEFDFHDDDA KGECFRKYNH PMYSFRDHSI FLSSRSRYKF LFNYRRNDYK
     KWAYGLRQAG YATDKKYPQK LIALIERYSL DDYDEEVVRG GLDTVREPKN YDVFTHEVEK
     GDTLYGISRE YSISVNELMR INNLDSTNLS IGQVINIRKE RSVK
//
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