ID A0A1I4Q8J4_9PSEU Unreviewed; 659 AA.
AC A0A1I4Q8J4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN05421805_1012 {ECO:0000313|EMBL:SFM36106.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFM36106.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFM36106.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFM36106.1,
RC ECO:0000313|Proteomes:UP000199398};
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; FOUP01000001; SFM36106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4Q8J4; -.
DR STRING; 455193.SAMN05421805_1012; -.
DR OrthoDB; 66275at2; -.
DR Proteomes; UP000199398; 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; cd06583; PGRP; 1.
DR Gene3D; 1.10.530.10; -; 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; IPR023346; Lysozyme-like_dom_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 SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 287..425
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 48..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 72080 MW; C8C3FB084AC11CF1 CRC64;
MAAREPQSST EDIRDGISEV AKTLTTRKPR WWRAAAVTAA ATGLLAGAAQ PAAGTSPDEP
RSTEQQAFES AAAEFGVPAP LLLATSYQLT RWEDHRGEQS KAGGYGPMHL TEVDFEQLRR
ENPKLRKLAD NPTLHTLTEA AELVDLPPEQ VKRDPAQNIR AGAALLAERA KQLGDGQLPN
TLGGWYPAVA ELSGSPQASG ARSFADSVYE VLDSGRSRTT STGQQVGFAK IPEVTPDRDL
TGTNLADVQA ARVEPKAECP AELDCKYIPA AYAPTDPEDP TGGYGNYDTA NRPKDVRINS
IVIHDTETSY QSTISLFQNP AHGSASHYVI RSSDGEVTQM VPTKDMAWHA GSWDRNMRSI
GIEHEGWAAE GGTWYTEQMY RSSAQLVKYL ADKYDIPLDR EHILGHDEVS ADKPEQAGGE
HYDPGPYWDW AHYMNLLDAP LDGDTGGDDV VTIFPRFDTN RPVVTECPPK EECRELPSQP
ANFLYLRSAP RDDAPLLSSA SVHPDGSPGT TRIEDWSAKA TVGRQYAVAE RRGDWLALWF
DGKKAWLRDP GGVNTAPADD AELVTPVRAD VPTYGMALPD ADEFPNGLDP LVIKPLPYKL
PQGQVYVAGR ASRAIYYNVG YDGVNDPNNH KVVLGGETYV PISYNHRWVY VKESDLEEA
//
