ID W1J8A4_9GAMM Unreviewed; 462 AA.
AC W1J8A4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-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:CDL85735.1};
GN ORFNames=XSR1_90074 {ECO:0000313|EMBL:CDL85735.1};
OS Xenorhabdus szentirmaii DSM 16338.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL85735.1, ECO:0000313|Proteomes:UP000019202};
RN [1] {ECO:0000313|EMBL:CDL85735.1, ECO:0000313|Proteomes:UP000019202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL85735.1,
RC ECO:0000313|Proteomes:UP000019202};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT 16338.";
RL Submitted (NOV-2013) 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 -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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:CDL85735.1}.
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DR EMBL; CBXF010000154; CDL85735.1; -; Genomic_DNA.
DR AlphaFoldDB; W1J8A4; -.
DR STRING; 1427518.XSR1_90074; -.
DR Proteomes; UP000019202; 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; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF6; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIB; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CDL85735.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019202}.
FT DOMAIN 291..449
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 174..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 49993 MW; 675D58F5C3D0B8B5 CRC64;
MKEDSTMLNA CFMNTLFVNR SVNKSVNRNK KWCTHGLITC ILFVMLSQLI MASAASAALS
STSALSNIHV SNRSSEATVT LEFTGEHPEY RFFSLHSPDR LVVDLRQAGK IAGLPMRLSG
QDLVRLVRSS QPPDSRHQRI VLELAHKATA SSSVKRIGGK SQVVIALKAH GAAGNTSVSK
NSVSHASSHE SKQLQTHAAP VAKATSDHPE KSVRKQTAQV QHGKGMSHIV VAIDAGHGGQ
DPGAIGQRGL KEKDVTISVA RKLEVLLRTD PMFKPILTRN GDYFISVAGR SEVARKHKAN
MLVSIHADAA PNRSAKGASV WVLSNRRANS ELGNWLEQHE KQSELLGGAG DALANGTDPF
LSQAVLDLQF GHSQRVGYDV AMQVLSQLIK IGSLHKRTPE HASLGVLRSP DIPSILVETG
FISNQSEEAL LGSTQYQEKL AQAIHLGLRQ YFQANPLQIA PK
//
