ID   F7JT69_9FIRM            Unreviewed;      1312 AA.
AC   F7JT69;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN   ORFNames=HMPREF0991_00332 {ECO:0000313|EMBL:EGN48819.1};
OS   Lachnospiraceae bacterium 2_1_58FAA.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=658082 {ECO:0000313|EMBL:EGN48819.1, ECO:0000313|Proteomes:UP000004820};
RN   [1] {ECO:0000313|EMBL:EGN48819.1, ECO:0000313|Proteomes:UP000004820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_1_58FAA {ECO:0000313|EMBL:EGN48819.1,
RC   ECO:0000313|Proteomes:UP000004820};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 2_1_58FAA.";
RL   Submitted (MAY-2011) 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:EGN48819.1}.
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DR   EMBL; ACTO01000002; EGN48819.1; -; Genomic_DNA.
DR   PATRIC; fig|658082.3.peg.340; -.
DR   HOGENOM; CLU_007147_0_0_9; -.
DR   OrthoDB; 2051435at2; -.
DR   Proteomes; UP000004820; Unassembled WGS sequence.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
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; 1.10.530.10; -; 1.
DR   Gene3D; 2.60.40.3760; -; 7.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR013688; GBS_Bsp-like.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404:SF5; AUTOLYSIN PH-RELATED; 1.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF08481; GBS_Bsp-like; 7.
DR   Pfam; PF01832; Glucosaminidase; 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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1312
FT                   /note="MurNAc-LAA domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038587705"
FT   DOMAIN          300..430
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          36..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1312 AA;  143017 MW;  5CF8488E94E6B8AA CRC64;
     MKKVQKVLAL LLVFMMVFTT AGMNVAAAGE MDSVAGEADI QSQEQPQTLD ETDTQQEATQ
     QTSEGILEYV YVDESVVNMP QTQNIAVGFS DENLVLESAV LHYSSVVTGE QFEMPASAIV
     NNTVLFTQDY PEGSAEDVYQ LDSLTYQSSG VSSTVNLLDE EIDAGYTVTV QPEEENSSEE
     AVPDVAVYSL SEDGNVIEAS SDTENIEETV AGVLEEADPV SPLAREARAN KTVVICAGHD
     ATHTGASGNG LKEEELTFKV AQYCKQALEQ YQGVTVYMDR DSISCKYPGQ STSYCLNQRI
     KDAAALGATV FVDIHFNTGG GTGAEVYYPN KSYNEGIHQE GQNLANKILS ELSALGLTNR
     GAKIKDGTTG ETDSNGNKDD YFTTNYLSKQ YGMTGVIVEH AFLDSASDAA KLKDENFLKK
     LGEADAAGIA ATYGFSKGDN GNEQATVQIK NKNDFNGTAQ IEVSGVGAGA QIAVWSDDNG
     QDDLKWYSVS GNSGTVNFDI KNHKKSAGTY NVHVYNSSST KILCNTTFRV SKDTSAKLKV
     SAVDGRQDLY RVKLSFADMP DEVSGVQFPV WSKGDQSDIR WITAQKTSSG VWEADVSISG
     YQIGDIYQVH AYASLTNGKQ VFIGNSTFKV VGPSADVTIK NYSAENGTFD VVVENIVAPA
     GVKEVQVPVW SLRGQSDIVW YRAEKQSDGT YKVGVDIANH KNNTGTYNIH IYILGNDGSQ
     TMVASTTQKV EASAVEITAK DETGKESQYE LTAKNVRNAD QVRFAVWSDV NGQDDLIWYD
     AKKKSSTWST EISIVNHKTA GVYNVHVYST VGKKQTLIGN TTFKVSSPTG TLEVKNYSES
     KGSFEVILKN VTSKSGVNAV YIPVWSESNQ SDIVWYQADK QSDGSYKVIV KTKNHNQNTI
     YNIHAYVTAK NGIMQFVDGT SKDVSKMEPK VSISNADGKE KKYTATIENA NALGKVSSVQ
     FAVWSDTNGQ DDLIWYQGTQ KNADAWSTEI EISNHKTAGS YNVHVYGMID GVQKFLVADT
     FEVSKPKGTI EVKNYNAAKG TFDVVVKNVS SKSGVQEVQI PVWSKEDQSD IVWYSAEKQG
     DGTYKAEVEL SRHQNNKGTY NIHVYILTET SIYAFVAGTT YEVSGNSSEQ NTENLTPIMG
     ESTTTVEQMM RYYESTGNQY PAEALGKGGA PTLRDFCQIY YDEATAEGVK AEVAFAQAMK
     ESAWLKFGGI VKIEQFNFAG LGALDGNSQG QAASFPDVRT GIRAQIQHLK AYASSEALKN
     ACVDPRFKYV TRNSAPYVEW LGIKENPSGT GWASSKNYGY QIVNMMDVLK NK
//