ID A0A1I2UB43_9GAMM Unreviewed; 447 AA.
AC A0A1I2UB43;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN05216175_11299 {ECO:0000313|EMBL:SFG74223.1};
OS Neptunomonas qingdaonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Neptunomonas.
OX NCBI_TaxID=1045558 {ECO:0000313|EMBL:SFG74223.1, ECO:0000313|Proteomes:UP000198623};
RN [1] {ECO:0000313|Proteomes:UP000198623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10971 {ECO:0000313|Proteomes:UP000198623};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FOOU01000012; SFG74223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2UB43; -.
DR STRING; 1045558.SAMN05216175_11299; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000198623; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..447
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011681501"
FT DOMAIN 401..444
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 447 AA; 49321 MW; F9A5769BD3C443CE CRC64;
MMKNLRKFTG CFLTIACLLV AGHVSAADIK NVRMWLAPDN TRLVFDLNGP VTHKIFSLNN
PDRLVLDING AAIKTRLSKL DLKGSPIKQV RSSMNGNNLR IVLDLNQMIR PRSFDLKPND
QYGHRLVLDL FNLEKETVVK TATPERKGAQ LRDIIIAIDA GHGGEDPGAI GAGRVREKDV
VLGIAKEVGR LIDNEKGFKA ELVREGDYYI SLRGRTKEAR KKNADLFVSI HADAFKDSRA
RGASVWVLSN RGATSEVGRW LAQKENSADL IGGVGSVSLE DKDDVLAGVL LDMSMTASRS
DSLQIASKIH GNVNKFAKMH KSRVESAGFM VLKSPDIPSI LVETGFISNP EEARLLKTKA
YQQKMAKAIY EGIKSHFWNK PPAYTYVAYE KNGGDKQSVQ RHYQVVSGDT LSVIASRHGI
ALNVLRKTND LKGDKIRIGQ VLRIPTS
//
