ID   A0A2A9CFF8_9BACI        Unreviewed;       335 AA.
AC   A0A2A9CFF8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Autolysin {ECO:0000256|ARBA:ARBA00032390};
DE   AltName: Full=Cell wall hydrolase {ECO:0000256|ARBA:ARBA00030881};
GN   ORFNames=ATG70_1267 {ECO:0000313|EMBL:PFG13078.1};
OS   Bacillus sp. es.036.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1761764 {ECO:0000313|EMBL:PFG13078.1, ECO:0000313|Proteomes:UP000222003};
RN   [1] {ECO:0000313|EMBL:PFG13078.1, ECO:0000313|Proteomes:UP000222003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=es.036 {ECO:0000313|Proteomes:UP000222003};
RA   Fredrickson J.;
RT   "Microbial Interactions in Extremophilic Mat Communities.";
RL   Submitted (OCT-2017) 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:PFG13078.1}.
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DR   EMBL; PDIZ01000001; PFG13078.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9CFF8; -.
DR   OrthoDB; 9812621at2; -.
DR   Proteomes; UP000222003; Unassembled WGS sequence.
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   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   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01471; PG_binding_1; 2.
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:0000313|EMBL:PFG13078.1}.
FT   DOMAIN          21..146
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01510"
FT   DOMAIN          194..251
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          298..334
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
SQ   SEQUENCE   335 AA;  37222 MW;  9939B50F887A5887 CRC64;
     MSNFEIITAD QVIEMLKGRK YSRAQVHHTW KPNHSDFNGK NHIALQESMY RYHVNVRGWD
     NIGQHLTLMP DGLFVTGRPF WSMPAGIKGY NTGAFMIEHL ANFDNGHDKL NGAQLNSSLK
     VYQYLVKECG AEIMFHNEHA AKSCPGTGVN RHDFIYSVLS YTPNQVEPKV ILHPTQEKVK
     SGVIEFVLGV GDAGKQVRDL QNKLKSLKYD IGKYGADGKF GRDTKAAVEK FQQDHGLVKD
     GLAGPNTFAE LKEAIAAEKY TKAKTVPSSA VVPYPGHLIK IGSRGKDVER IQRAVGVKVD
     GIYGPNTASE VRNYQERHGL SVDGIVGPNT WNTLF
//