ID Q65EU3_BACLD Unreviewed; 359 AA.
AC Q65EU3; Q62QB2;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE AltName: Full=Autolysin {ECO:0000256|ARBA:ARBA00032390};
DE AltName: Full=Cell wall hydrolase {ECO:0000256|ARBA:ARBA00030881};
GN OrderedLocusNames=BL01582 {ECO:0000313|EMBL:AAU25048.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU25048.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU25048.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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; CP000002; AAU25048.1; -; Genomic_DNA.
DR RefSeq; WP_011198301.1; NC_006322.1.
DR AlphaFoldDB; Q65EU3; -.
DR STRING; 279010.BL01582; -.
DR KEGG; bli:BL01582; -.
DR PATRIC; fig|279010.13.peg.3655; -.
DR eggNOG; COG3409; Bacteria.
DR eggNOG; COG5632; Bacteria.
DR HOGENOM; CLU_047675_1_0_9; -.
DR Proteomes; UP000000606; Chromosome.
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; 1.10.101.10; PGBD-like superfamily/PGBD; 2.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
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; PF01471; PG_binding_1; 2.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 2.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000606}.
FT DOMAIN 14..168
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 176..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 39029 MW; 57CDAAD1E02D6742 CRC64;
MVKVVKNYVK VNQYTRPGLK LAGVKGIVMH WTATPGASAL NERNYFNGTC IADKRYASAH
YFVDRKEAQH IIPENEVAYH AHDQNRCYVS FLKPNANTTA IGVEMCVEKD GKIHSQTIQN
AAELVADLCK RYGLSTNKIV RHYDVTNKSC PTPWVRDASQ LTTFRKKVDA LLGNNTVSKT
TSSTSQSSKS TGTILKKGAS GSQVKALQKR LIAAGFSLPK YGADGSYGNE TVQAVKALQK
KAGIAVDGIY GPATEKALAA IEAKKKKSSS SGKKSSYTLP SGIYKVKSPM MKGTAVWQIQ
EALAALYFYP DKEAKNNGID GYYGPKTANA VKRFQLMHGL SADGIYGPKT KAKIEALLK
//
