ID A0A0Q5RCK1_9SPHN Unreviewed; 359 AA.
AC A0A0Q5RCK1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ASG11_06875 {ECO:0000313|EMBL:KQS04007.1};
OS Sphingomonas sp. Leaf357.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS04007.1, ECO:0000313|Proteomes:UP000051080};
RN [1] {ECO:0000313|EMBL:KQS04007.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04007.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS04007.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04007.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQS04007.1}.
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DR EMBL; LMPM01000001; KQS04007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5RCK1; -.
DR STRING; 1736350.ASG11_06875; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000051080; 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:UP000051080}.
FT DOMAIN 195..349
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 359 AA; 38905 MW; 23D93118F507D307 CRC64;
MVFDWTAPVP ARQYIRVSLI LALLACWFAG TPALATMVDG VDVTRDRVVV RFDQRLADAT
ALVVVEPNRF AREVMGANPS AIGASGARRP ELTLDLSTLG AAPRRYEVSR KVPKAIRTLA
LPRVYGDDDS RPLVVIDAGH GGMDPGAISQ ADGLREKDVT LRIARAIRDE LLKSGRVRVA
LTREDDRFLV LQERYGIARR LKASLFISIH CDSVGSGLAS GASVYTLSEV ASDKESAKLA
ARENKADIIA GLDLGGAPAD ISSILIDLTQ RETMNASANF ARLLGREAQP LIPLKPNFHR
MASLIVLKAP DMPSILFETG YISNPSDAAF IDSAEGRKRI AESVRRAVEV HFARRLAAN
//
