ID   A0A1Q7TA71_9BACT        Unreviewed;       398 AA.
AC   A0A1Q7TA71;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN   ORFNames=AUG81_12770 {ECO:0000313|EMBL:OLD85414.1};
OS   Verrucomicrobia bacterium 13_1_20CM_4_54_11.
OC   Bacteria; Verrucomicrobiota.
OX   NCBI_TaxID=1805408 {ECO:0000313|EMBL:OLD85414.1, ECO:0000313|Proteomes:UP000185599};
RN   [1] {ECO:0000313|EMBL:OLD85414.1, ECO:0000313|Proteomes:UP000185599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLD85414.1}.
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DR   EMBL; MNIL01000158; OLD85414.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7TA71; -.
DR   Proteomes; UP000185599; 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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..398
FT                   /note="MurNAc-LAA domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011960171"
FT   DOMAIN          189..324
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          377..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  43236 MW;  B538FE79A0A9C77B CRC64;
     MVLPVKRWFA IAFLAGAIAI SQATALAADD WQIIKLSGQD YLSVDNISRF YGLPAGIAAS
     GEKVEFEAAK NPLEFVSGSR EVMINGARSW LCFPAIEQNG KLLVSRTDVA KTIEPLVRPH
     RVPNVGKVQT IVVDPGHGGY DKGQVSRYGY EKDFALDVAR KLRPLLLSKG LRVIMTREGD
     YFVPLEVRAQ IANKARDSIF VSIHFNASND DRNATGFEIF SFTPRGAPST SDSAVAPSAL
     STQPGSAVDA QSLALSACIY HSLLGHIPEY DRGIKRARFA VLRLTKVPAV LIEGGFLTEQ
     GQCRLIAQKE WRAKLAHAIS VGIESYRALG IKKQPPLLVA DYRKQIKSAP NEFVVQDAEL
     KEADTSIVNL VGQSAFPAPQ QAPTSSQRVS LESAPIVP
//