ID A0A1M4VLL3_9RHOB Unreviewed; 398 AA.
AC A0A1M4VLL3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN05444273_102302 {ECO:0000313|EMBL:SHE69941.1};
OS Litoreibacter ascidiaceicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1486859 {ECO:0000313|EMBL:SHE69941.1, ECO:0000313|Proteomes:UP000184144};
RN [1] {ECO:0000313|EMBL:SHE69941.1, ECO:0000313|Proteomes:UP000184144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100566 {ECO:0000313|EMBL:SHE69941.1,
RC ECO:0000313|Proteomes:UP000184144};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQUV01000002; SHE69941.1; -; Genomic_DNA.
DR RefSeq; WP_073141174.1; NZ_FQUV01000002.1.
DR AlphaFoldDB; A0A1M4VLL3; -.
DR STRING; 1486859.SAMN05444273_102302; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000184144; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..398
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012567327"
FT DOMAIN 230..385
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 398 AA; 43277 MW; 394E8836EBE65904 CRC64;
MSRLISLIAL ASLGMTMSAA SQDLRALARV DMDASRVTDS RGSTTLSLAL TQAVPYRVQV
FDAPNRIAVD FREVSFEPDL SGLDRSDRIA ELRAGTIRDG WSRLVMELSE PMLVENAGMQ
TDPQDGDAVI TVTLAPATQS DFSEHAKSTV TKLTAWQQEQ ITSNGDTRRM VVVDPGHGGV
DPGAQRAGVD EADLMLQFAR ELREQLLRSG RYDVIMTRED DSFVSLPQRV SLARAAGADV
FISLHADALA EGRATGTTIY TLSDEASDEA SANLAERQDR TDILAGVDLT AQDDQIATVL
MDLARRETTP RTDRLAEALV DGLRNTLGKL HKRPRLEAGF SVLKAPDIPS VLIELGFMSS
ERDLDRLQDQ VWRSQAAAGI VDALDLWALE DDAIAAGR
//
