ID A4J255_DESRM Unreviewed; 451 AA.
AC A4J255;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Cell wall hydrolase/autolysin {ECO:0000313|EMBL:ABO49158.1};
GN OrderedLocusNames=Dred_0618 {ECO:0000313|EMBL:ABO49158.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO49158.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO49158.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO49158.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000612; ABO49158.1; -; Genomic_DNA.
DR RefSeq; WP_011876995.1; NC_009253.1.
DR AlphaFoldDB; A4J255; -.
DR STRING; 349161.Dred_0618; -.
DR KEGG; drm:Dred_0618; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_10_0_9; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000001556; 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; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR036582; Mao_N_sf.
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 Pfam; PF11741; AMIN; 1.
DR Pfam; PF07833; Cu_amine_oxidN1; 2.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABO49158.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..451
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002670747"
FT DOMAIN 336..444
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 451 AA; 50108 MW; 5A44002994852E92 CRC64;
MKKLISTIIT ICFLLTVTPA LAKTPELIIN NQPVKSDVSP QIIDGRVLVP LRVISESLGA
LVDWEKDSQT VKIQDQHKTL RLQLQNKITY VNDQPLELDV PPLMLDNRTM VPLRFISEQL
GARVSWIGTE KKVIIERSEN NSVKDGPTSV PADRKLTNVS YEETEEKSVI EIEVKEGTNK
VFELKNPDRI VFDLMDTANE VSADPEVNSQ FIDAIKLGVH PGNVTRVVIQ LKDRKTTAYE
AKQMADKLVV TLTRREAPPP EEGYTHKVVN GQSNVIVIDP GHGGKDVGTV GASGRWEKMV
NLAIADKLKG ILQNEGFTVV MTREDDASFL SLDERAQLAN KSDPLCFISI HANAAENKAV
SGLETYSFYG SDKTLANLIH NAVLARTNQV NRKVKEAGFY VIKHTKMPSV LIETGFVSNS
EEENFLFNEN NQMAIAEGIA EAVKQFKSLY K
//
