ID A0A075R4G9_BRELA Unreviewed; 371 AA.
AC A0A075R4G9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=BRLA_c024140 {ECO:0000313|EMBL:AIG26734.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG26734.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG26734.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG26734.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00001561};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CP007806; AIG26734.1; -; Genomic_DNA.
DR RefSeq; WP_003337661.1; NZ_CP007806.1.
DR AlphaFoldDB; A0A075R4G9; -.
DR STRING; 1042163.BRLA_c024140; -.
DR KEGG; blr:BRLA_c024140; -.
DR eggNOG; COG3023; Bacteria.
DR HOGENOM; CLU_015278_0_0_9; -.
DR Proteomes; UP000005850; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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; 1.10.530.10; -; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AIG26734.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850}.
FT DOMAIN 215..346
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 371 AA; 42261 MW; A270B0CA7A33EF9C CRC64;
MKRQAINLII LCTLLSTLLS SIPSFITNPT VVYASPQSQQ ELVKWFKEAA DEYNVPITLL
ISIGWIESML DDHDGEPNNM NGYGFMNLMS NPKRKTLEEA SEITGISTDE LKTSTQSNIK
GGAAILAKYQ QDITKNKNHS KDYKDWVEAV KLYSGADSDE VRTHYAEDVF SLIENGFIDL
SSEKLIKLPS ENSKEYKGKK VLPQLDIKWI SAHESNYDST RRSAKDITHL VIHVMQGTYA
GSIDWAQRDH GSMGASSAHY YVSDDGDITQ MVDDRNVAYH ARSANPYTIG IEHEGYIDDP
KWFTNIMYRE SAKLAAKLAY TYDIPISRRH IKGHSEYPNQ THTDPGGYWD WDYYMKNIKV
YHDKFVNDGR K
//
