ID A0A095AXK0_9SPHN Unreviewed; 303 AA.
AC A0A095AXK0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=FG91_01747 {ECO:0000313|EMBL:KGB54847.1};
OS Sphingopyxis sp. LC81.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1502850 {ECO:0000313|EMBL:KGB54847.1, ECO:0000313|Proteomes:UP000029574};
RN [1] {ECO:0000313|EMBL:KGB54847.1, ECO:0000313|Proteomes:UP000029574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC81 {ECO:0000313|EMBL:KGB54847.1,
RC ECO:0000313|Proteomes:UP000029574};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (MAY-2014) 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:KGB54847.1}.
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DR EMBL; JNFD01000015; KGB54847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095AXK0; -.
DR STRING; 1502850.FG91_01747; -.
DR PATRIC; fig|1502850.3.peg.1773; -.
DR eggNOG; COG0860; Bacteria.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000029574; 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; 3.40.630.40; Zn-dependent exopeptidases; 1.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KGB54847.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..303
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001905070"
FT DOMAIN 139..293
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 303 AA; 32529 MW; 405EC2660BF50CF7 CRC64;
MSLLALLGMI ATPPAAIAGR PIVDPAFDRP RIERPVSAGF RAKRPGKRYS VTVPIGKPKP
SVALPRIEGP ANDRLPLVVI DAGHGGHDPG AISPHSGKRE KDITLALARA IRADLLASGR
VRVALTRADD RFLVLEERYG IARRLKADLF ISVHADAAEN SQASGASIYT LSEVASDREA
ARLAARENKA NVINGVDLGA HSGDVSAILL DLTQRETMNV ASDFARLLQR EASGDVKFRT
TAHRFASFIV LKAPDTPSVL FETGFISNKD DSKFLASSAG QKKVARGVRN AVQVHFARRI
VAR
//
