ID G4F8K6_9GAMM Unreviewed; 487 AA.
AC G4F8K6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=HAL1_13651 {ECO:0000313|EMBL:EHA14944.1};
OS Halomonas sp. HAL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA14944.1, ECO:0000313|Proteomes:UP000005692};
RN [1] {ECO:0000313|EMBL:EHA14944.1, ECO:0000313|Proteomes:UP000005692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX PubMed=22156396; DOI=10.1128/JB.06359-11;
RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA Wang G., Rensing C.;
RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL J. Bacteriol. 194:199-200(2012).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHA14944.1}.
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DR EMBL; AGIB01000062; EHA14944.1; -; Genomic_DNA.
DR RefSeq; WP_008958616.1; NZ_CP130610.1.
DR AlphaFoldDB; G4F8K6; -.
DR PATRIC; fig|550984.5.peg.2630; -.
DR Proteomes; UP000005692; 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;
FT DOMAIN 441..484
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 158..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 53106 MW; 701ABA958D8D2F00 CRC64;
MEMKAAAARV LRLLAVSFFA LVAVDVQASS VESMRLWAAP DHARLVFDLS AATNANVFSL
QNPARLVIDL DDTQMDTDPS TLPLHDSAIT SVRTGKREGG GLRVVLELNR AIEPRHFTLT
PNDQYGHRLV VDLEYPGESA VENPIDPIEA MIREQEIQAQ RASTQAQLPG SVEPPRNEAP
AAVQEAKPHP RRDIIIAVDA GHGGEDPGAI GPSGTREKDV VLEIARRLAS EVNGTEGFKA
VLVRDGDYYL GLRQRTALAR EQKADFFVSV HADAFTSPRP QGSSVYALSQ RGATSETAQW
LADSENRSDL IGGVDGSLSL RDKDQVLRGV LLDLTMTATL NDSLSIGGQV LEQLGRVNRL
HKSRVEQAGF MVLKSPDIPS LLIEVGFISN PDEERRLRDP VHQGGLSQAI FSGLREHFQR
YPPPASLLAW QRDNQRSPAG NEYRIQSGDT LSAIAVRHGV PVNQLKQAND INGDVIRVGQ
VLQIPRS
//
