ID A0A0Q0JCQ0_9GAMM Unreviewed; 435 AA.
AC A0A0Q0JCQ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:KPZ70159.1};
GN ORFNames=AN944_02543 {ECO:0000313|EMBL:KPZ70159.1};
OS Shewanella sp. P1-14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ70159.1, ECO:0000313|Proteomes:UP000050414};
RN [1] {ECO:0000313|EMBL:KPZ70159.1, ECO:0000313|Proteomes:UP000050414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ70159.1,
RC ECO:0000313|Proteomes:UP000050414};
RA Gilbert D.G.;
RL Submitted (OCT-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:KPZ70159.1}.
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DR EMBL; LKTL01000015; KPZ70159.1; -; Genomic_DNA.
DR RefSeq; WP_055024964.1; NZ_LKTL01000015.1.
DR AlphaFoldDB; A0A0Q0JCQ0; -.
DR PATRIC; fig|1723761.3.peg.2605; -.
DR Proteomes; UP000050414; 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 Hydrolase {ECO:0000313|EMBL:KPZ70159.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050414};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..435
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006181838"
FT DOMAIN 389..432
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 435 AA; 47671 MW; FBB6A3E091025B9D CRC64;
MTRFFSFVLL FGFSLIVEAA NKLDSIRVWD APDSTRVVLD LSQAPDYSYF SLSNPQRLVI
DLKQASTKVK FDDIAKNSKL INKVRLSKPP KAGTLRLVLE LASPVKANLF SLTPTAPYGN
RLVVDLDNSA NKPAAKKQVV QTSKRSKDVI VAIDAGHGGE DPGSIGPKGT YEKKVVLAIS
KRLARKINET PGMKAVMTRS GDYFVNLNQR SELARNSRAD LLLSIHADAF TSPQPKGASV
WVLSKRRANT EIGRVFEDKE KHSELLGGVG DIIQNTDSEQ YLVMTLIDMS MDHSMAESHS
IATDILAGLG KVTKLHKNKP ESASFAVLKS TDIPSILIET GFISNPKEER LLLDGNHQQK
LANAIHKGVV NYFEANPPSG TMFAKQSNVK HTVRSGESLS VIAQRYKVSV ASIKKSNNLK
SDVLRIGQKL VIPRA
//
