ID A0A0E4GD11_9FIRM Unreviewed; 240 AA.
AC A0A0E4GD11;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=1016 {ECO:0000313|EMBL:CFX32984.1}, 375
GN {ECO:0000313|EMBL:CFX06681.1};
OS Syntrophomonas zehnderi OL-4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX32984.1, ECO:0000313|Proteomes:UP000045545};
RN [1] {ECO:0000313|EMBL:CFX32984.1, ECO:0000313|Proteomes:UP000045545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL-4 {ECO:0000313|EMBL:CFX32984.1,
RC ECO:0000313|Proteomes:UP000045545};
RA Strepis Nikolaos;
RL Submitted (MAR-2015) 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; CGIH01000004; CFX06681.1; -; Genomic_DNA.
DR EMBL; CGIH01000018; CFX32984.1; -; Genomic_DNA.
DR RefSeq; WP_046495099.1; NZ_CGIH01000018.1.
DR AlphaFoldDB; A0A0E4GD11; -.
DR STRING; 690567.1016; -.
DR OrthoDB; 9794294at2; -.
DR Proteomes; UP000045545; 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:UP000045545}.
FT DOMAIN 201..240
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
SQ SEQUENCE 240 AA; 26609 MW; 0C44586E64AFE79D CRC64;
MNLHKLILTN NACYKAGKTI IPKGIMVHST GANNPWLKRY VGPDDGLLGK NQYNNHWNQD
KPGGRQVCVH AFIGKLANGT VATYQTLPWN YRGWHGGSGS KGSVNDTHIS FEICEDGLTD
AAYFNAVYKE AAELCAYLCK EYKLDPMADG VIIGHYEGHK RGIASNHADP GHWFPKHRKS
MDTFRAEVKK LLSVTEVTTT TDPKKLYRVQ VGAYSVKANA DAMLKKVKAA GFKDAFIKYS
//
