ID A0A0N0V4D8_9RHOB Unreviewed; 406 AA.
AC A0A0N0V4D8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiC_1 {ECO:0000313|EMBL:KPA22921.1};
GN ORFNames=shim_12110 {ECO:0000313|EMBL:KPA22921.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA22921.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA22921.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA22921.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-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:KPA22921.1}.
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DR EMBL; LAJH01000009; KPA22921.1; -; Genomic_DNA.
DR RefSeq; WP_054001649.1; NZ_LAJH01000009.1.
DR AlphaFoldDB; A0A0N0V4D8; -.
DR STRING; 1389006.shim_12110; -.
DR PATRIC; fig|1389006.3.peg.1243; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000037951; 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:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 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 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KPA22921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037951};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..406
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005860702"
FT DOMAIN 236..391
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 406 AA; 43692 MW; 943BAF232BF79096 CRC64;
MSRVLAIVAA LFLSGAGWAQ EFSALARLDA EKSSLQSGWR GAVTLEVSLS QGVPWRVFHL
DGPRRLVVDF REVDWGAAQP EDFGSVEGVG TVRFGGYRPG WSRMVLDLEA PLSLDSAEME
VPEGTGAATL RISLTPTTAE DFAANAGAPH DPRWDLPQPE DVGQAREDKP DWAPTVVVID
PGHGGIDPGA ERDGTQEKEL MLSFARELRD TLRRAGGFEV FMTRDEDSFV SLERRVAFAH
QKNADVFISL HADSLSQGHA HGAAVYTLSA EATDAASALL AERHDRADIL SGVDLSGADD
EVTDVLLDLA RLETEPRTAT LADIMVGALR EATGAVNKKP RREGAFSVLK AADVPSILIE
LGFMSSEGDL ANLQDAGWRA SMSAGIRDGL QAWVIEDKAT RALVRQ
//
