ID R9LGE7_9FIRM Unreviewed; 598 AA.
AC R9LGE7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN ORFNames=C814_02466 {ECO:0000313|EMBL:EOS57446.1};
OS Anaerotruncus sp. G3(2012).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=1235835 {ECO:0000313|EMBL:EOS57446.1, ECO:0000313|Proteomes:UP000014129};
RN [1] {ECO:0000313|EMBL:EOS57446.1, ECO:0000313|Proteomes:UP000014129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G3(2012) {ECO:0000313|Proteomes:UP000014129};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anaerotruncus bacterium G3.";
RL Submitted (APR-2013) 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:EOS57446.1}.
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DR EMBL; ASTA01000071; EOS57446.1; -; Genomic_DNA.
DR RefSeq; WP_016317119.1; NZ_KE159678.1.
DR AlphaFoldDB; R9LGE7; -.
DR STRING; 1235835.C814_02466; -.
DR PATRIC; fig|1235835.3.peg.2598; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_456097_0_0_9; -.
DR OrthoDB; 9772024at2; -.
DR Proteomes; UP000014129; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR013783; Ig-like_fold.
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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000014129};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..598
FT /note="MurNAc-LAA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004476686"
FT DOMAIN 488..594
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 598 AA; 63179 MW; EBFBB3EB8287111B CRC64;
MQKKQIKNRL VSFVLVLAVC VGVSVAPAAA QGGYNDLEAI TGHVSLTIPQ GLTVSRPSGQ
ITTTDAAYFI AGTSDPGLPL TLNGQEVEQR GVRGSFGVYV ALDAGTNRFV LEQGSAREEV
IIVRGNASAE AATTTVISRM APAYDCATFS GETITLSCVA PSGASVTASI GNRQVTLEQS
AATAKAGVPA TFTAKLTAGE VSGTKDLGQV VYTLNGQTDF ESEGRVYITG SGSRLAVQVK
NDATVVYSDA QRSRFIDTAK LGGIDTVKDI NGDLYELSTG GWVPREAMQP LTEEVPLRLS
VEQALFGATD DGNGEVYSFP GSARPMVRSY QDSEKLFVRL CNTTMSSDAV SELKAAVSNS
RVFGGVAVSQ KDGYADLTFQ LSGNRTLWGY DITYGREGGI NVFAKYKPSL QQGSRPLAGI
TIAVDAGHGG SDPGAVGVPG TKAAMEKDIN LATAIAVQKR LESLGATVLM TRSEDENPPI
NDRMQGTVDA DLFISLHCNS ISYDRDTNKA GGTEVYYYED QSQRLAQILA ANVADYTGRT
NRGAKFSAFR VTLNTYAPAV LVEMGFLTNP AEYDSMTSRS GIFRTANAVG DGVLAVFR
//