ID A0A248TJX3_9BACI Unreviewed; 362 AA.
AC A0A248TJX3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=CKF48_14620 {ECO:0000313|EMBL:ASV68429.1};
OS Cytobacillus kochii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX NCBI_TaxID=859143 {ECO:0000313|EMBL:ASV68429.1, ECO:0000313|Proteomes:UP000215137};
RN [1] {ECO:0000313|EMBL:ASV68429.1, ECO:0000313|Proteomes:UP000215137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BDGP4 {ECO:0000313|EMBL:ASV68429.1,
RC ECO:0000313|Proteomes:UP000215137};
RA Wan K.H., Yu C., Park S., Hammonds A.S., Booth B.W., Celniker S.E.;
RT "Complete Genome Sequence of Bacillus kochii Oregon-R-modENCODE STRAIN
RT BDGP4, isolated from Drosophila melanogaster gut.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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DR EMBL; CP022983; ASV68429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248TJX3; -.
DR KEGG; bko:CKF48_14620; -.
DR OrthoDB; 9794294at2; -.
DR Proteomes; UP000215137; 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:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF11; N-ACETYLMURAMOYL-L-ALANINE AMIDASE XLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF158634; RPA2825-like; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Competence {ECO:0000256|ARBA:ARBA00023287};
KW Reference proteome {ECO:0000313|Proteomes:UP000215137};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT DOMAIN 13..161
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 166..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 39648 MW; 3D9B453F4C179532 CRC64;
MVNVIKQLVS QEVVNQRSYG KGNKIQYITP HQTGNMGIGA NAQMHANLQS NLNSRQASWH
YQVDDRMVIQ SFEDDVMCWA AGDGRGPGNT ASIHIEMCIN ADGDYEQTIN NGAALVKMLM
DKYGLDRSRI KQHHDWSGKN CPAQLRAGYK GITWEDFLNK VDGVQEEENF GSPSPGPNQP
KPKPKPVENG NSIVDYLNAQ GIDSSFKNRA ILAKQYGMNN YQGTAAQNIA LLEKIKKGVP
KKPQIAPKAN LNVDGKWGKS TTRALQKALG TPVDGIISNQ PKNSVTNAFY DGTIHFASGK
QGSPMVKALQ RMIGANPDGF MGPHTVRALQ IYLGTVVDGV LSRPSLVVKE MQRRLNAGTF
VK
//
