ID A0A0G9HEF6_9GAMM Unreviewed; 549 AA.
AC A0A0G9HEF6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=BJI69_12225 {ECO:0000313|EMBL:APG06513.1}, Y883_07180
GN {ECO:0000313|EMBL:KLD67574.1};
OS Luteibacter rhizovicinus DSM 16549.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1440763 {ECO:0000313|EMBL:APG06513.1, ECO:0000313|Proteomes:UP000182987};
RN [1] {ECO:0000313|EMBL:KLD67574.1, ECO:0000313|Proteomes:UP000035585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16549 {ECO:0000313|EMBL:KLD67574.1,
RC ECO:0000313|Proteomes:UP000035585};
RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT "A phylogenomic and molecular marker based taxonomic framework for the
RT order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT containing the genus Rhodanobacter and its closest relatives.";
RL Antonie Van Leeuwenhoek 107:467-485(2015).
RN [2] {ECO:0000313|EMBL:APG06513.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LJ96 {ECO:0000313|EMBL:APG06513.1};
RX PubMed=28123952;
RA Aamot H.U., Hofgaard I.S., Lysoe E.;
RT "Complete genome sequence of Luteibacter rhizovicinus strain LJ96T,
RT isolated from the rhizosphere of barley (Hordeum vulgare L.) in Denmark.";
RL Genom Data 11:104-105(2016).
RN [3] {ECO:0000313|Proteomes:UP000182987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LJ96T {ECO:0000313|Proteomes:UP000182987};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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; CP017480; APG06513.1; -; Genomic_DNA.
DR EMBL; JPLB01000023; KLD67574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G9HEF6; -.
DR STRING; 1440763.BJI69_12225; -.
DR KEGG; lrz:BJI69_12225; -.
DR PATRIC; fig|1440763.5.peg.1233; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000035585; Unassembled WGS sequence.
DR Proteomes; UP000182987; 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:KLD67574.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..549
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014228173"
FT DOMAIN 503..546
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 131..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 57147 MW; CF6A3424B55F52CA CRC64;
MRGMTIKLGL LACVTAIATL TAVAVSAADV KAARAWAGPE YTRVVFDLSG PAAYKMSQGD
VPGSVVLDIA GSSVTGDFSA PGGQGLFKSM SVSKQGGSAR LVATVDPRAK PKSFLLKPAG
DYGYRLVLDL YPGGQSDPGD NPPPAADHDS PSVASAGNDD DAEASAPAQA PLPTRGSRNS
RSKSVPAGKP PMLPTGDRKV VVAIDAGHGG EDPGAKGATG LREKDVTLQV ARELADQINR
QPGMQAVLTR NGDYFIPLKR RYEIAREHNA DMFVSIHADA FKNGDAKGSS VWVLSPRGKT
SEASRWLADR ENRADLVGGV SLDDKDDSLA AVLLDLQQGY AMQASESIAG NVLKALGRLG
PTHRGYVERA NFVVLRSPDV PSILVETAFI TNPAEETRLR DDGHRRELAT AVLGGVRNYF
ESMPPPGTWF AAQAARRNGG SLASTAASAP AAPAVAADAG AVASDAVKAA TRATPPRKTL
ARADTTASVA KASNGRADDN VRDLHRVNRG ETLTGIANQY GVSVGALKMA NKMNDDNVRI
GSVMVIPSG
//
