ID A0A268EA33_9BACI Unreviewed; 328 AA.
AC A0A268EA33;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Autolysin {ECO:0000256|ARBA:ARBA00032390};
DE AltName: Full=Cell wall hydrolase {ECO:0000256|ARBA:ARBA00030881};
GN ORFNames=CHH83_06230 {ECO:0000313|EMBL:PAD69992.1};
OS Bacillus sp. 7586-K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD69992.1, ECO:0000313|Proteomes:UP000216230};
RN [1] {ECO:0000313|EMBL:PAD69992.1, ECO:0000313|Proteomes:UP000216230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7586-K {ECO:0000313|EMBL:PAD69992.1,
RC ECO:0000313|Proteomes:UP000216230};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-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:PAD69992.1}.
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DR EMBL; NPCL01000017; PAD69992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268EA33; -.
DR OrthoDB; 2812205at2; -.
DR Proteomes; UP000216230; 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 CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR33734:SF35; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 1; 1.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Reference proteome {ECO:0000313|Proteomes:UP000216230};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..328
FT /note="Autolysin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013397647"
FT DOMAIN 29..72
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 74..117
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 328 AA; 37300 MW; DFDA5200DCC8D921 CRC64;
MKKHFLLIIC LIYCLVIVAN SAYAQRPSNL YEVKPDDTLS KIAQKYHTSI ADLKLYNGLQ
ANTVTEGQKL LVPITYTVRS GDTLEHLSST FQLSSEAIKK ANRLSSDQLQ KGQQLRIVPK
KLSMHGQHIV MTREQFKTWL ENNTFNRKIT LIQHHHTWLP SYKDFTGNNH FAMLEGMENF
HRKNMNWKTI AQNLTTFPDG TIAVSRPFNI APEGSIGNKA NDAGLMIENI GNFDIGHDVM
TKKQKDTIVY MTALLCLKFG LTPSIDSITY HHWWNLKTGE RVLDNAKSFD VKTCPGTGFF
GGNTTTSAKK YFYPLIQKQM NEISSTFE
//