ID K0NJF6_DESTT Unreviewed; 586 AA.
AC K0NJF6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=AmiC: N-acetylmuramoyl-L-alanine amidase amiC {ECO:0000313|EMBL:CCK80003.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:CCK80003.1};
GN Name=amiC {ECO:0000313|EMBL:CCK80003.1};
GN OrderedLocusNames=TOL2_C18420 {ECO:0000313|EMBL:CCK80003.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK80003.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK80003.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
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DR EMBL; FO203503; CCK80003.1; -; Genomic_DNA.
DR RefSeq; WP_014957344.1; NC_018645.1.
DR AlphaFoldDB; K0NJF6; -.
DR STRING; 651182.TOL2_C18420; -.
DR KEGG; dto:TOL2_C18420; -.
DR PATRIC; fig|651182.5.peg.2198; -.
DR HOGENOM; CLU_014322_11_0_7; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CCK80003.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..586
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003837665"
FT DOMAIN 424..575
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 586 AA; 65924 MW; 4919621D72DB2884 CRC64;
MRRFKPLIRS ISFFMMLFSG VFIFPANGPA DTAKGKYLIA DSCYKKLRNS PVKKRLESEW
LNCISRYESI YKLHPRSSWA PAGMYKAAQL YLTLSKLSGK KSHKSQAEDL LARINNKYPE
SAYGKRAKSL LKSIDANPKL YTKEIRHLKS KKNLTKNDSL IKKFNQAQKQ AIEKKSSLNK
PHYQKPSAIK PVPVKEIFSR DTTIADLRFW SNPEYTRIVV NADKESDYSH RLLKKDPGID
KPFQRLYIDI EQSKLGNGVA EYTPINDNLL KQARAGQYLP HTVRVVIDIK SFENYKIFSL
KDPFRIVIDV WGKGSNGGTV PPSGQRIASL GKPEKPEKFS RITTDNLKSS DIARQLALGV
NKIVIDPGHG GADPGAPGYF KNVWEKDIVL KLAKKLAGIL RERLNCTVLL TRSTDKKLTL
EERTAIANTK KADLFISLHC NAAKNRRAKG IETYILNLAT DEQAIAVAAR ENATSEKNIS
DLEYILSDLM KHAKIEESTR LANVVHNSFV NGMKKRYSGI TDLGVKQAPF YVLLGARMPS
ILVEASFLSN KTECKRLMSD SYQTSICNAI ADGVTKYIDA TNPKQL
//
