ID A0A1G9ZGP3_9GAMM Unreviewed; 497 AA.
AC A0A1G9ZGP3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN04487951_10386 {ECO:0000313|EMBL:SDN19746.1};
OS Halomonas arcis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=416873 {ECO:0000313|EMBL:SDN19746.1, ECO:0000313|Proteomes:UP000199677};
RN [1] {ECO:0000313|Proteomes:UP000199677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6494 {ECO:0000313|Proteomes:UP000199677};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FNII01000003; SDN19746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9ZGP3; -.
DR STRING; 416873.SAMN04487951_10386; -.
DR Proteomes; UP000199677; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000199677}.
FT DOMAIN 451..494
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 167..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54149 MW; BB55D2193956E728 CRC64;
MVVSAMGISA RVMQALALRQ VALSVVAIIS AGLWTSLQAA TVEGMRLWAA PDHARLVFDL
SGPSSANVFS LDGPARLVID LEDSQLEADP DSLSLEDSAI STVRTGTRNG NGLRVVLELN
REVEPRHFTL APNDQYGHRL VVDLEYPGES AVENPIDPIE AMIRDQEMEA QRASAQVGDS
EQASSPADEP RVSEEARPHP RRDIIIAVDA GHGGEDPGAI GPSGTREKDV VLDISQRLAN
TINAVDGFKA VLIRDGDYYL GLRQRTQLAR EQKADFFVSI HADAFNSPRP QGSSVYALSQ
RGATSETAQW LADSENRSDL IGGVDGSLSL RDKDQVLRGV LLDLTMTATL NDSLSIGGQV
LDQLKRVNRL HKSRVEQAGF MVLKSPDIPS LLIETGFISN PDEERRLRDP VHQQQIAEAI
FSGLKRHFER YPPPASLLAW QRDNQGRPSG DEYRIQSGDT LSAIAVRHGV PINQLKQAND
LNGDVIRVGQ VLRIPSS
//
