ID A0A1T5J950_9MICO Unreviewed; 737 AA.
AC A0A1T5J950;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN04324258_1145 {ECO:0000313|EMBL:SKC47782.1};
OS Krasilnikoviella flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Krasilnikoviella.
OX NCBI_TaxID=526729 {ECO:0000313|EMBL:SKC47782.1, ECO:0000313|Proteomes:UP000189777};
RN [1] {ECO:0000313|EMBL:SKC47782.1, ECO:0000313|Proteomes:UP000189777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21481 {ECO:0000313|EMBL:SKC47782.1,
RC ECO:0000313|Proteomes:UP000189777};
RA Peterson S.W.;
RL Submitted (FEB-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; FUZQ01000002; SKC47782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5J950; -.
DR STRING; 526729.SAMN04324258_1145; -.
DR OrthoDB; 9758772at2; -.
DR Proteomes; UP000189777; 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; 2.60.40.2700; -; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000189777};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..737
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012866158"
FT DOMAIN 258..396
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 242..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 77203 MW; EAA1419FA6F2F67F CRC64;
MRSVRRRTIG LAAAGLLVPL VTIPAVAAGA GPSTAPTSGV TCDAVVAAPD RESVFAAASD
ATGVPADLLK AVSYMESRWD QHAGTPSADG GYGLFNLLDH APEAPDGAGK DATPRAPVSE
LDRAAALTGL SVADLKSDAG ANTCGAAALL ASYQEDAGRG ADGGLASWDA AVARMSDAPT
FADRVFSTLR QGGARTTDDG GRVTLAARAD AVLPESASAA TSDPAADCPP DLGCEWLPAP
YEKASPGLPD DTGDYGNHDQ ADRTGEGGPS IDYIVIHDTE TAYEPSVRLV TDPTYLAWNY
TLRSSDGHVA NHLEPGDVGW HAGNWYMNMH SIGLEHEGWA GTSGWFTEAM YQSSAELVRH
LAGEYDIPLD RAHVIGHDQI PGILPGSTKN VHWDPGPYWD WEHYFELLGA PIGDGLSPTS
DVAPGDVVEV VAGYTDNANP VTGCAQASPG SGDCVKGAGT NFVVAHQGPS LDAPYARDPG
WKPGGADGTT YASDISARVT SGHKLVVAQV QDQWLGVWWA GSLVWIHNPA DRPVVVPSTG
QTVTVSGDAA AAVYGRAYPE GAAYAPYPGI TPQAVTPIEY TIGAGQTYVV SDDTVTTDYY
NAKSFDGSIP DDRTDVRGED AYYQLWYAHR QVFTRAADVT LHDPVVTDVE GPGIVGRAQI
GKVLRVDVGE YLPGSDDTEV DVQWLRDGDP VRGADGSRYH LTGRDRGAEI SVEVTVSAHG
YTSATFTSDT VGPVRPH
//
