ID   A0A1I1Q464_9FLAO        Unreviewed;       374 AA.
AC   A0A1I1Q464;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:SFD16787.1};
GN   ORFNames=SAMN05216297_10568 {ECO:0000313|EMBL:SFD16787.1};
OS   Flavobacterium phragmitis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=739143 {ECO:0000313|EMBL:SFD16787.1, ECO:0000313|Proteomes:UP000199672};
RN   [1] {ECO:0000313|EMBL:SFD16787.1, ECO:0000313|Proteomes:UP000199672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10370 {ECO:0000313|EMBL:SFD16787.1,
RC   ECO:0000313|Proteomes:UP000199672};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOMH01000005; SFD16787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1Q464; -.
DR   STRING; 739143.SAMN05216297_10568; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000199672; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..374
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011503923"
FT   DOMAIN          90..249
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          257..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  41679 MW;  2A05BE186DE8FE5B CRC64;
     MNRINKFKVI FTLSLTFLSF YAQSQSNVFK VTLDAGHGDH DFGAVYSGRI EKNIALAIVL
     KVGKILELNP NVNVIYTRKT DVFIDLVERA NIANRANSNI FVSIHCNANK NTAADGTETY
     VMGLSKVASN LEAAKKENSV ITLEKDYKRK YEGYDPNSPE SMIGMTLMQE EYLDNSISLA
     TKIEDNFEKL GKKLRQGGVK QAPFMVLHKA YMPRVLVETG FISNPTEGNI LNSEEGQDDI
     ARAIAEAILS YKREYFGSGG ETEESRPIKD TSTPAKPKTT TPVTAVKNAP KGIFFKVQLI
     ASIKKTPLEP KNFKGLKNVT MLFENNIYKY FYEETSSYET AQKYLQEAKS KGYGAAFLVA
     TKDGEKISIQ DAIK
//