ID A0A0W0VD36_9GAMM Unreviewed; 461 AA.
AC A0A0W0VD36;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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 Name=amiB {ECO:0000313|EMBL:KTD17529.1};
GN ORFNames=Ljor_1835 {ECO:0000313|EMBL:KTD17529.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD17529.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD17529.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD17529.1,
RC ECO:0000313|Proteomes:UP000055035};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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};
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:KTD17529.1}.
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DR EMBL; LNYJ01000011; KTD17529.1; -; Genomic_DNA.
DR RefSeq; WP_058471275.1; NZ_RDQQ01000012.1.
DR AlphaFoldDB; A0A0W0VD36; -.
DR STRING; 456.Ljor_1835; -.
DR PATRIC; fig|456.5.peg.1958; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000055035; 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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000055035};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..461
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006914702"
FT DOMAIN 414..457
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 461 AA; 50826 MW; 1A2BAECADEF07118 CRC64;
MNLRALVGFC FFMLACFPAF AAKLLSIEIR QQNGAPSVLF TLDKAIPHRV FTLTNPNRVV
IDFENTDLAL NLNHVNLGRE LIKYIRSGHP NPHTLRLVFE VNQMVLTQTK LLQQTAAKHS
FSLALQTKDR MQKPASGKAS FPITGKQTVV KSRQAAPVLV HHAPPSRGLR DVIVVLDPGH
GGKDPGASGP RRTAEKNVTL AIAQKLKQII DRQPGMKAVL TRNGDYYIEL RDRLKIARKY
NADVFISIHA DAFINQHSSG ASVFALSQSG ATSEAARWLA EKENYSELGG VNLSELDDQS
GLVRTVLIDL SQTATIGASL HMGERVLRNL DHITNLHNRK VEQARFMVLK SPDIPSILIE
TGFISNPREE SNLTNSAYQT RLTQAIFEGL KHYFWDYPPH GTRIEAMAGA GSNNIHLVQR
GESLPLIAAK YHVSVASLKT VNHLSGSQIK AGQKLVIPDM A
//
