ID K4L544_9FIRM Unreviewed; 623 AA.
AC K4L544;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase domain-containing protein {ECO:0000259|SMART:SM00644};
GN ORFNames=DCF50_p2399 {ECO:0000313|EMBL:AFV06402.1};
OS Dehalobacter sp. CF.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV06402.1, ECO:0000313|Proteomes:UP000000482};
RN [1] {ECO:0000313|EMBL:AFV06402.1, ECO:0000313|Proteomes:UP000000482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AFV06402.1};
RX PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA Tang S., Gong Y., Edwards E.A.;
RT "Semi-automatic in silico gap closure enabled de novo assembly of two
RT dehalobacter genomes from metagenomic data.";
RL PLoS ONE 7:E52038-E52038(2012).
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DR EMBL; CP003870; AFV06402.1; -; Genomic_DNA.
DR RefSeq; WP_015044432.1; NC_018867.1.
DR AlphaFoldDB; K4L544; -.
DR STRING; 1131462.DCF50_p2399; -.
DR KEGG; dec:DCF50_p2399; -.
DR PATRIC; fig|1131462.4.peg.2418; -.
DR eggNOG; COG2247; Bacteria.
DR eggNOG; COG5632; Bacteria.
DR HOGENOM; CLU_426943_0_0_9; -.
DR Proteomes; UP000000482; Chromosome.
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; cd14670; BslA_like; 1.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 2.60.40.3490; -; 1.
DR Gene3D; 3.40.50.12090; -; 2.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR007253; Cell_wall-bd_2.
DR InterPro; IPR034650; YuaB-like.
DR InterPro; IPR038480; YuaB-like_sf.
DR PANTHER; PTHR30032:SF8; AMIDASE ENHANCER; 1.
DR PANTHER; PTHR30032; N-ACETYLMURAMOYL-L-ALANINE AMIDASE-RELATED; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF17735; BslA; 1.
DR Pfam; PF04122; CW_binding_2; 3.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000482};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..623
FT /note="N-acetylmuramoyl-L-alanine amidase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038366386"
FT DOMAIN 464..596
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 623 AA; 67901 MW; E07C6B61DDC2E1BC CRC64;
MLCFLFFTGW MTSAANADTT QIDRIYGSDR YATAAAISQK GWESSEYAVL ARGDDFADAL
CAGPLAAKYH APILLTESQS LNADARSEIQ RLGVKRVFIT GGTSSISAEI ETTLREAGVI
EIVRLAGKDR YETSVKIAEA LNSNKMILAT GKNYPDALSI AVVAAQAEIP ILLAGKDRLP
QSVKEYVQRQ TTQQAYIVGG TGVISEGVAQ QVPGAFRLAG SDRYATNVAV LEHFSGQLDL
SRLFVAVGEG PKGTEFADAL TGAVLAAKSS SPLILVRDTL PEVTQKYLKG KITPFTVVTG
LGGENAVRSS VLQRIINLAN TNDGKLSVSP ASTIAGATKN IYLVYLPGEN MNNGTVEFFL
PDRYLAIAGQ DKITINGTMN SLTSEQISDA GRRVKISGLN VTTGQKIILT LNDKSVQDVG
NYSFKVIADA DGSGILRPSS GSLTESRTLP VRFPSLKVGI QLLSYNRPTT PLSPKGFVIH
STADPGATAQ KIVQYFNYPN RYSSTHYVAD WTETVQMIQE DEMAWHAAQT ANQRYLSVEM
CEPEGNQPEQ FKKVWDQTVL LVADACIRYG WDPQEDIFSH MDISYAYRET DHIDPIPFLK
KYNKTWQDLL KAIQAKMVEL QTN
//
