ID B9J6I2_BACCQ Unreviewed; 352 AA.
AC B9J6I2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Autolysin {ECO:0000256|ARBA:ARBA00032390};
DE AltName: Full=Cell wall hydrolase {ECO:0000256|ARBA:ARBA00030881};
GN OrderedLocusNames=BCQ_PT15 {ECO:0000313|EMBL:ACM15977.1};
OS Bacillus cereus (strain Q1).
OG Plasmid pBc53 {ECO:0000313|EMBL:ACM15977.1,
OG ECO:0000313|Proteomes:UP000000441}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM15977.1, ECO:0000313|Proteomes:UP000000441};
RN [1] {ECO:0000313|EMBL:ACM15977.1, ECO:0000313|Proteomes:UP000000441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1 {ECO:0000313|EMBL:ACM15977.1,
RC ECO:0000313|Proteomes:UP000000441};
RC PLASMID=pBc53 {ECO:0000313|EMBL:ACM15977.1,
RC ECO:0000313|Proteomes:UP000000441};
RX PubMed=19060151; DOI=10.1128/JB.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
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DR EMBL; CP000229; ACM15977.1; -; Genomic_DNA.
DR AlphaFoldDB; B9J6I2; -.
DR KEGG; bcq:BCQ_PT15; -.
DR HOGENOM; CLU_047675_2_0_9; -.
DR Proteomes; UP000000441; Plasmid pBc53.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR23208; LYSOZYME PROTEIN; 1.
DR PANTHER; PTHR23208:SF36; LYSOZYME-RELATED; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF08239; SH3_3; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Plasmid {ECO:0000313|EMBL:ACM15977.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..352
FT /note="Autolysin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039075129"
FT DOMAIN 34..168
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT DOMAIN 211..270
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
SQ SEQUENCE 352 AA; 39317 MW; 008B78E9972A8EFC CRC64;
MKKPLKLFSS LFMTLLLLFS FATASFADRV LIIQDLPKQA YRYGVGAYEG VVAHSTATPE
APAINIQRYE SRTWRSAFVH YAVDWDETIQ IADTKYIAYG AGPAANKRFV HVELSETSNP
AKFKSSYERY VKLLAKILKD RGIHPSKGLW THKDITYKLG GTDHEDPLDY LRSHGVSESQ
FRADVQRAYE GATVTVKPKS QEPSQNVTWT TGVAYIDGYN VNLRSGPSTN YGIIRQLSKG
ESYQVWGKQG DWLNLGGNQW IYNNPSYIKY QGEQTSAASS VVGKRVVSKV DNLRFYDAAS
WADKDVAGTV DEGLGFTIDA KVSVNGSAQY KVHNSKGTTF YITANESYVY VK
//