ID A0A0R0DLG7_9GAMM Unreviewed; 501 AA.
AC A0A0R0DLG7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ABB34_13580 {ECO:0000313|EMBL:KRG82841.1};
OS Stenotrophomonas daejeonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=659018 {ECO:0000313|EMBL:KRG82841.1, ECO:0000313|Proteomes:UP000050940};
RN [1] {ECO:0000313|EMBL:KRG82841.1, ECO:0000313|Proteomes:UP000050940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16244 {ECO:0000313|EMBL:KRG82841.1,
RC ECO:0000313|Proteomes:UP000050940};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG82841.1}.
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DR EMBL; LDJP01000088; KRG82841.1; -; Genomic_DNA.
DR RefSeq; WP_057641910.1; NZ_LDJP01000088.1.
DR AlphaFoldDB; A0A0R0DLG7; -.
DR STRING; 659018.ABB34_13580; -.
DR PATRIC; fig|659018.3.peg.2933; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000050940; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000050940};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..501
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006395977"
FT DOMAIN 313..468
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 136..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 51199 MW; 0F8FE3C28A6D61DB CRC64;
MPTAIRLPVL SALVAGLGLA ACASAWAGEV RGVALQAGAT GTHAEIQLAG GGGYKTLSLS
APNRLVVDFP DSSAVRGLKL PAATGVVTAV RTGNPVPGTF RVVFDLAESV TAFKPRMQAS
GAESKLVIEW PGDAPASAAT ATAPAPTPAT TAPPPAQNDA AARAEAARAT AALTASVLQQ
ANAPAPATAT QEARPSPAAI LNGLTVATGV PATVPAASTP AQVTAAEPPA PRPVMPSDAS
RITMQPGMRT LVVAIDPGHG GQDPGAIGPT GKREKDVTLA VARELARQVN ATPGLRAYLT
RDTDVFIPLP MRAQRARAAK ADIFISIHAD AAENRSATGS SVYVLSTKGA SSQRARWLAD
KENAADLIGG VSLQRTEGTL ANVLLDLAQS GYMKASEDAA GHVLGGLKRI GNNHKPNLER
ANFAVLRTSD MPAMLVETAF ISNPEEERRL IDPAYQRRIA GAVLDGVHTF FSRQPPPGTL
FAARAQAEME AAAGTVAGGS K
//
