ID A0A095B829_9SPHN Unreviewed; 317 AA.
AC A0A095B829;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=FG95_00570 {ECO:0000313|EMBL:KGB58900.1};
OS Sphingopyxis sp. LC363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB58900.1, ECO:0000313|Proteomes:UP000029625};
RN [1] {ECO:0000313|EMBL:KGB58900.1, ECO:0000313|Proteomes:UP000029625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC363 {ECO:0000313|EMBL:KGB58900.1,
RC ECO:0000313|Proteomes:UP000029625};
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:KGB58900.1}.
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DR EMBL; JNFC01000004; KGB58900.1; -; Genomic_DNA.
DR RefSeq; WP_052182022.1; NZ_JNFC01000004.1.
DR AlphaFoldDB; A0A095B829; -.
DR STRING; 1120705.FG95_00570; -.
DR PATRIC; fig|1120705.3.peg.572; -.
DR eggNOG; COG0860; Bacteria.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000029625; 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 Reference proteome {ECO:0000313|Proteomes:UP000029625};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..317
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001913089"
FT DOMAIN 153..307
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 317 AA; 33856 MW; E37296839E143F5F CRC64;
MSPLLVLIGM IGAPPAALPA PAGAIHVDPR PASVGEFDPA SRGPGGELQP FTGFRAKRPE
KRYSVTVPIG KPKPAVTLPR IEGPADASLP LVVIDAGHGG HDPGAISPHD GSHEKDITLA
LARAIRKDLL ASGRVRVALT RSDDRFLVLE ERYGIARRLK ADLFISVHAD AAENQDASGA
SIYTLAEVAS DREAARLAAR ENKANIINGV DLGAHSGDVS AILLDLTQRE SMNVASDFAR
LLQREASDEV KFRTTAHRFA SFIVLKAPDT PSVLFETGFI SNKDDVEFLA SPAGQKKIAR
GVREAVQIHF ARRNVAR
//
