ID A0A1Q3KZB3_9BACT Unreviewed; 311 AA.
AC A0A1Q3KZB3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN ORFNames=BGN96_03415 {ECO:0000313|EMBL:OJU38280.1};
OS Bacteroidales bacterium 45-6.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1895719 {ECO:0000313|EMBL:OJU38280.1, ECO:0000313|Proteomes:UP000185892};
RN [1] {ECO:0000313|EMBL:OJU38280.1, ECO:0000313|Proteomes:UP000185892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=45-6 {ECO:0000313|EMBL:OJU38280.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJU38280.1}.
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DR EMBL; MKRS01000776; OJU38280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3KZB3; -.
DR Proteomes; UP000185892; Unassembled WGS sequence.
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; 2.
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; 2.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00257; LysM; 2.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022638};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 266..310
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 311 AA; 36177 MW; E90806F72AB58AF4 CRC64;
MKKFEKENFR LFRIYALSAF VLFCFVGFAA APKRLKIYEE YIEKYKDVAR KHQAKYKIPS
SITLAQGLLE SGAGKSDLAI KSNNHFGIKC HNDWKGATVI AKDDKPDDCF RKYDRVEDSY
EDHSLFITQK PRYRKLFDLQ ITDYKGWATG LQTAGYATDK AYANKLIKVI EDYELFVYDV
SSGKNKKHTT KEQPQVLLYS HTPYKTFGLV YVIAKRGDTF EAIAQEFGFK AKDLYKYNEV
PEDFPLSEGD LVYFEKKRKK AESPYYEHVV KVGESMHSIS QLYGIQVKSL YKMNKQDMEY
VPTEGDVLRL R
//
