ID A0A1I5FWN2_9FIRM Unreviewed; 240 AA.
AC A0A1I5FWN2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN04489757_11636 {ECO:0000313|EMBL:SFO28228.1};
OS Anaerocolumna aminovalerica.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerocolumna.
OX NCBI_TaxID=1527 {ECO:0000313|EMBL:SFO28228.1, ECO:0000313|Proteomes:UP000198806};
RN [1] {ECO:0000313|EMBL:SFO28228.1, ECO:0000313|Proteomes:UP000198806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1283 {ECO:0000313|EMBL:SFO28228.1,
RC ECO:0000313|Proteomes:UP000198806};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; FOWD01000016; SFO28228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5FWN2; -.
DR STRING; 1527.SAMN04489757_11636; -.
DR OrthoDB; 9794294at2; -.
DR Proteomes; UP000198806; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0042834; F:peptidoglycan binding; 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 InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
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; PF05036; SPOR; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF110997; Sporulation related repeat; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000198806}.
FT DOMAIN 201..240
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
SQ SEQUENCE 240 AA; 26513 MW; 52045BF964F3586F CRC64;
MNLHKLILTN NACYKAGRTI TPKGIMVHST GANNPNLKRY VGPDDGLLGK NQYNNHWNQD
KPDGRQVCVH AFIGKLADGS IATYQTLPWN HRGWHGGSGS KGSVNDTHIS FEICEDGLTD
AAYFNAVYKE ATELCAYLCK EYKLDPMADD VIIGHYEGHK RGIASNHADP GHWFPKHGKS
MDTFRAEVKK LLSAIEAPTS TDPKKLYRVQ VGAYSVKANA DAMLKKVKAA GFKDAFIKYS
//
