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Database: UniProt
Entry: A0A1T4MQH4_9GAMM
LinkDB: A0A1T4MQH4_9GAMM
Original site: A0A1T4MQH4_9GAMM 
ID   A0A1T4MQH4_9GAMM        Unreviewed;       493 AA.
AC   A0A1T4MQH4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=SAMN02745674_00544 {ECO:0000313|EMBL:SJZ69213.1};
OS   Lysobacter spongiicola DSM 21749.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1122188 {ECO:0000313|EMBL:SJZ69213.1, ECO:0000313|Proteomes:UP000190061};
RN   [1] {ECO:0000313|EMBL:SJZ69213.1, ECO:0000313|Proteomes:UP000190061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21749 {ECO:0000313|EMBL:SJZ69213.1,
RC   ECO:0000313|Proteomes:UP000190061};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUXP01000001; SJZ69213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4MQH4; -.
DR   STRING; 1122188.SAMN02745674_00544; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000190061; 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   Reference proteome {ECO:0000313|Proteomes:UP000190061}.
FT   DOMAIN          307..462
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   493 AA;  50490 MW;  0E9940A5F82CF90A CRC64;
     MRADRAILQT FILGLALLVG LLTGVSKANE IKGLTVSSGA TGTRAEIALA EAGDFNIIKL
     SGPDRLVVDL AGTSIAGGVQ VPSGAGVVSR VRTGQPVPGT ARVVFDLGET VAPLQPRIEQ
     GASGPKLVVE WPDDGAARLA TENTGATATP APAPATSADP IDQAAASSEA TSRLISEIAA
     RAMAQQPAAA STGSAAQVSL PPVPTTVATG VPTPAPGAAP AREQPAATPA KTLQQVMQGT
     PMRPLVIAID PGHGGQDPGA IGKSGTREKD VVLEISRELA RQINATPGMR AYLTRDRDVF
     IPLNKRASLA RSAGADMFIS IHADAAENRA ADGSSVYVLS LKGASSQRAR WLANKENAAD
     LVGGARLPQN NDTLTSVLLD LTQSGNMKAS EEAAGEILDG LKRVGNIHKP QIERANFAVL
     RTSDIPAMLV ETAFISNPEE ERRLQDPGFR RKVAGAVLDG INTFFTRQPP PGTLYAARAA
     TGGGAAGAAG GSP
//
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