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Database: UniProt
Entry: A0A494X9W4_9BURK
LinkDB: A0A494X9W4_9BURK
Original site: A0A494X9W4_9BURK 
ID   A0A494X9W4_9BURK        Unreviewed;       666 AA.
AC   A0A494X9W4;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN   ORFNames=D7S89_20575 {ECO:0000313|EMBL:RKP45226.1};
OS   Trinickia fusca.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Trinickia.
OX   NCBI_TaxID=2419777 {ECO:0000313|EMBL:RKP45226.1, ECO:0000313|Proteomes:UP000280434};
RN   [1] {ECO:0000313|EMBL:RKP45226.1, ECO:0000313|Proteomes:UP000280434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7MK8-2 {ECO:0000313|EMBL:RKP45226.1,
RC   ECO:0000313|Proteomes:UP000280434};
RA   Gao Z.-H., Qiu L.-H.;
RT   "Paraburkholderia sp. 7MK8-2, isolated from soil.";
RL   Submitted (OCT-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:RKP45226.1}.
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DR   EMBL; RBZV01000010; RKP45226.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494X9W4; -.
DR   OrthoDB; 8776734at2; -.
DR   Proteomes; UP000280434; 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   Gene3D; 2.10.70.40; peptidoglycan hydrolase; 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   PRINTS; PR01002; FLGFLGJ.
DR   SMART; SM00257; LysM; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000280434}.
FT   DOMAIN          318..362
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          263..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   666 AA;  71018 MW;  8DF87B844C396196 CRC64;
     MAYTYEDKLQ FIQNLYCAAR QVSDETGCSW QLILAQAALE TGWGEKTLHG TNNIFNIKAD
     KSWKGESKVF HVQEEKADGS MVWVDDPFRV YPSILESLRD RQKFLAENPR YRENGLFDPG
     TKGNLLKEAT ALRRAHYATK DDYPQKLQGM FECKSMQKAI ARAQKEGCKG CLPTLNIYVL
     DGARVKLEGA KVKASQNGKT LELVADKDGH VQIQAALSNG KVTIEVWSEH DKTWVPAEQD
     SKPSTPPTAL TFIAPTFAVQ TSTDHHEPVA AAKGASVPAA ASSTPAAPAG AASGAGAGGG
     KASAGASHTQ TAHHPGTTTY KVKKGDSLIK IAKAHSTSYL TIARLNGISS PYYLHPGQEL
     KMPKPAHHDA TPAAHAGNAQ QHAAQSSPAV ASQPVVPPSA SQSQAASQPQ AASQSEGAAQ
     SATPPASSPM SQTTPQAASH ASAASSASSG QSASGSQAAA GPTILVPDNT VHAVRYRSEA
     DHPQTDVISA RRAPWMAVAE QEFHAHVRRS HKGEEQNKNI KEYFSATSLH VNSDQLAYCA
     AFVNWCLARS GYKGNNSAGA ATLAHWGRAT RDNKPAYGAV AIVRIPPQGV YHVTFIRGKV
     ARSRHALNLG TLGGNQGHDH VVSHSSVPAS WVTHYRFPEE YTESDEDYDL AFVDVDGATM
     TAASTR
//
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