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Database: UniProt
Entry: A0A1J6X1B4_9BACI
LinkDB: A0A1J6X1B4_9BACI
Original site: A0A1J6X1B4_9BACI 
ID   A0A1J6X1B4_9BACI        Unreviewed;       264 AA.
AC   A0A1J6X1B4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   05-FEB-2025, entry version 25.
DE   SubName: Full=Peptidoglycan-binding protein {ECO:0000313|EMBL:OIU71929.1};
GN   ORFNames=BHE18_04595 {ECO:0000313|EMBL:OIU71929.1};
OS   Rossellomorea aquimaris.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Rossellomorea.
OX   NCBI_TaxID=189382 {ECO:0000313|EMBL:OIU71929.1, ECO:0000313|Proteomes:UP000182062};
RN   [1] {ECO:0000313|EMBL:OIU71929.1, ECO:0000313|Proteomes:UP000182062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAMM {ECO:0000313|EMBL:OIU71929.1,
RC   ECO:0000313|Proteomes:UP000182062};
RA   Waghmode S.R., Suryavanshi M.V.;
RT   "Bacillus aquimaris SAMM genome sequence reveals colonization and
RT   biosurfactant production capacities.";
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:OIU71929.1}.
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DR   EMBL; MINN01000074; OIU71929.1; -; Genomic_DNA.
DR   RefSeq; WP_071617594.1; NZ_MINN01000074.1.
DR   AlphaFoldDB; A0A1J6X1B4; -.
DR   OrthoDB; 9798935at2; -.
DR   Proteomes; UP000182062; Unassembled WGS sequence.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR   CDD; cd22786; DPBB_YuiC-like; 1.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 3.10.350.10; LysM domain; 2.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR051933; Resuscitation_pf_RpfB.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR39160; CELL WALL-BINDING PROTEIN YOCH; 1.
DR   PANTHER; PTHR39160:SF6; CELL WALL-BINDING PROTEIN YOCH; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF01476; LysM; 2.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF54106; LysM domain; 2.
DR   PROSITE; PS51782; LYSM; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000182062};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..264
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039179669"
FT   DOMAIN          27..70
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          74..117
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          120..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  28136 MW;  F0139B3CF2DADCB5 CRC64;
     MKLKKSIISV AAFTTLAVSG GASASAQEIE VKKGDTLWGL AKEYGTSVDQ LKTWNNLGSD
     VIFPDQELKV SSKEYYTVKK GDTLWAIASN YGISVDNLQG WNALESDLIV PGQELLINLD
     DKAPSTPANT SEQEEAAPAP QPEEKPEVAP EVEEASAEPQ QEQEAVANEL SVEATAYTAD
     CEGCSGITAT GVNLKENPDA KVIAVDPDVI PLGSKVYVEG YGYATAEDTG GAIKGNRIDV
     FIPSQDQAVD WGRKTVNVKV LETK
//
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