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Database: UniProt
Entry: A0A1M3M9N0_9BACT
LinkDB: A0A1M3M9N0_9BACT
Original site: A0A1M3M9N0_9BACT 
ID   A0A1M3M9N0_9BACT        Unreviewed;       397 AA.
AC   A0A1M3M9N0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN   ORFNames=BGP01_09175 {ECO:0000313|EMBL:OJX88505.1};
OS   Paludibacter sp. 47-17.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC   Paludibacter.
OX   NCBI_TaxID=1895899 {ECO:0000313|EMBL:OJX88505.1, ECO:0000313|Proteomes:UP000183960};
RN   [1] {ECO:0000313|EMBL:OJX88505.1, ECO:0000313|Proteomes:UP000183960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47-17 {ECO:0000313|EMBL:OJX88505.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJX88505.1}.
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DR   EMBL; MKVT01000020; OJX88505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3M9N0; -.
DR   STRING; 1895899.BGP01_09175; -.
DR   Proteomes; UP000183960; 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;
FT   DOMAIN          97..255
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          266..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   397 AA;  43808 MW;  9AD2386D05583032 CRC64;
     MKIKVRIFSL PFLLTLLILL VGAEVAGLVA QQRNFVLVLD AGHGGRDPGA VGKIAREKDV
     TLSVVRKVGA MVNAAMPDVK VVYTRKTDMF VPLEERASIA NNHHADLFIS VHTNAAKSRA
     AYGAETYTLG LAKSQSNLAV AMAENSVMML EDDYKTRYQG FDPSSVDSYI MFEFMMDTYL
     DNSIAFATDV QKQLTTHSRR HDRGVRQAGF WVLHRSACPS VLVELGFISN QQEELYMASE
     RGQQEMAESI YNAFVKYKKV YDRKSGNGGK VTAARPVTTP AEQAPAETPA VQPAKSSDTV
     EAQTPAVDPP QHLPVYKVQI ASSPTALKAG DRVFKGVKNV EFYKEGGLYK YTVGNETDFN
     TANRLKNEMR KHFPDAFVIA FVGDKKIPVS DALKIKK
//
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