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Database: UniProt
Entry: I9L7I8_9SPHN
LinkDB: I9L7I8_9SPHN
Original site: I9L7I8_9SPHN 
ID   I9L7I8_9SPHN            Unreviewed;       289 AA.
AC   I9L7I8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=WSK_0952 {ECO:0000313|EMBL:EIZ80394.1};
OS   Novosphingobium sp. Rr 2-17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ80394.1, ECO:0000313|Proteomes:UP000004732};
RN   [1] {ECO:0000313|EMBL:EIZ80394.1, ECO:0000313|Proteomes:UP000004732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732};
RX   PubMed=22933764; DOI=10.1128/JB.01159-12;
RA   Gan H.M., Chew T.H., Hudson A.O., Savka M.A.;
RT   "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline Crown
RT   Gall-Associated Bacterium Isolated from Vitis vinifera L. Grapevine.";
RL   J. Bacteriol. 194:5137-5138(2012).
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:EIZ80394.1}.
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DR   EMBL; AKFJ01000012; EIZ80394.1; -; Genomic_DNA.
DR   RefSeq; WP_008993909.1; NZ_AKFJ01000012.1.
DR   AlphaFoldDB; I9L7I8; -.
DR   PATRIC; fig|555793.3.peg.956; -.
DR   eggNOG; COG0860; Bacteria.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000004732; 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:UP000004732}.
FT   DOMAIN          125..280
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   289 AA;  30085 MW;  DEB25E93278325AE CRC64;
     MSRSLRYALL LSVPLSLAVA AIVLLRAGSL GAADQDYVVR FDMPSADAPV GLPRIDGPPD
     ASRPLVVIDP GHGGFDPGAG QGALKEKTVA LQVALALRRQ LLDAGGLRVA LTRDTDRFIA
     LSDRPDMARR LGADLFVSIH ADSAPEEGAR GASVYILSEK GSSEAATRFA ARENGADLVN
     GVRLSPRNAG VNAILLDLAQ RGAQAGSAQA ASLMLRELGD AKLGLHRERP EAAALAVLKA
     LDIPSLLFET GYINNPADAQ VLGSRQGQEA LAGAAARAIR AYFARTTGL
//
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