ID E4PHX8_MARAH Unreviewed; 452 AA.
AC E4PHX8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiC {ECO:0000313|EMBL:ADP98266.1};
GN OrderedLocusNames=HP15_2502 {ECO:0000313|EMBL:ADP98266.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP98266.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP98266.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00001561};
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DR EMBL; CP001978; ADP98266.1; -; Genomic_DNA.
DR RefSeq; WP_014577795.1; NC_017506.1.
DR AlphaFoldDB; E4PHX8; -.
DR STRING; 225937.HP15_2502; -.
DR KEGG; mad:HP15_2502; -.
DR PATRIC; fig|225937.3.peg.2527; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_014322_2_3_6; -.
DR Proteomes; UP000007077; 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; cd00118; LysM; 1.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_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; PF01476; LysM; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADP98266.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..452
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003185802"
FT DOMAIN 406..449
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 452 AA; 48903 MW; 72A17AC55F74CEC2 CRC64;
MNCAKLSKQL VWPIALLLVT LAFHGSAATQ VESARIWPAP DHTRLVLDTG GQVEHNIFSL
SGPARLVIDL KNANLKTDFS GLDLSGSPIK RIRSAPRNGT DLRVVLDLKA DIKPRSFQLE
PNQQYGHRLV VDLIDESGSR LEKATTPTVT QDSSGKRDVI VVIDAGHGGE DPGAIGPRGT
REKDVVLKMA KTLANLINDR PGYTAKLTRT GDYYIGLRNR TILARKYSAD LFVSVHADAF
RTPQPKGASV FALSQRGATS ETARWLANSE NRSDLIGGAG GLSLDGRDDM LAGVLLDLSM
TASINASLGV GSSVLGKLGG VAKLHKPGVE QAAFAVLKSP DIPSILVEAG FISNPQEEKN
LATEWYRNKL AGAIMKGIDD YFQKTPPPGT LLAWQKQNRQ GENSISHYRI QRGDTLSGVA
RKNQTTVSEL MQFNDLRDDR VMVGQTIRIP AS
//