ID A0A143HGY1_9BACL Unreviewed; 254 AA.
AC A0A143HGY1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidoglycan-binding protein {ECO:0000313|EMBL:AMX00751.1};
GN ORFNames=ATY39_16020 {ECO:0000313|EMBL:AMX00751.1};
OS Rummeliibacillus stabekisii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX NCBI_TaxID=241244 {ECO:0000313|EMBL:AMX00751.1, ECO:0000313|Proteomes:UP000076021};
RN [1] {ECO:0000313|EMBL:AMX00751.1, ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|EMBL:AMX00751.1,
RC ECO:0000313|Proteomes:UP000076021};
RX PubMed=27231360;
RA da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT from Antarctic Soil.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP014806; AMX00751.1; -; Genomic_DNA.
DR RefSeq; WP_066791456.1; NZ_CP014806.1.
DR AlphaFoldDB; A0A143HGY1; -.
DR STRING; 241244.ATY39_16020; -.
DR KEGG; rst:ATY39_16020; -.
DR OrthoDB; 9798935at2; -.
DR Proteomes; UP000076021; Chromosome.
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; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR39160:SF6; CELL WALL SHAPING PROTEIN YABE-RELATED; 1.
DR PANTHER; PTHR39160; 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:UP000076021};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..254
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007509294"
FT DOMAIN 26..69
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 75..118
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 129..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 254 AA; 26373 MW; 358ED35475DE979A CRC64;
MKKYLIALAG VFALGTAALT TQASAASYKV EKGDTLWSIS QDEEVSVKDL KKLNNLSSDI
IVPKQKLNTG KNEEKSYKIK KGDTLYKIAT EKGVSVGDLK AINGLAGDTI YVGQTLALTG
DKVEAASTQQ VEPKAANPVA AAPAKSAAQQ QPSTQPSSGK TMTVTATAYT PNCAGCSGVT
ATGVNVKANP HMKLIAVDPS VIPLGSKVWV EGYGTAIAAD TGGAIKGHKI DLLMPNNSQA
NSWGVRTVTI KVLN
//
