ID A0A0S8C556_9PROT Unreviewed; 423 AA.
AC A0A0S8C556;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=AMJ67_07445 {ECO:0000313|EMBL:KPK18990.1};
OS Betaproteobacteria bacterium SG8_41.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK18990.1, ECO:0000313|Proteomes:UP000051544};
RN [1] {ECO:0000313|EMBL:KPK18990.1, ECO:0000313|Proteomes:UP000051544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_41 {ECO:0000313|EMBL:KPK18990.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK18990.1}.
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; LJTT01000020; KPK18990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8C556; -.
DR STRING; 1703391.AMJ67_07445; -.
DR PATRIC; fig|1703391.3.peg.2832; -.
DR Proteomes; UP000051544; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..423
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006643557"
FT DOMAIN 250..405
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 153..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 46687 MW; EBC6ECAECCDCF76D CRC64;
MWQAARPLAL VLLALPAAAE NLEVAAARIW PSEEYTRVTL ESPSPLQYRI FGLKDPERLV
LDLEEVEVSA ALRDLIEKVG ANDPHVAGVR IGRFKPGVVR LVFDLKKEIR PQAFRLAPIG
DYGHRLVLDL YPTEAHDPLL AFLDSLDAER AALAGTSGAS EPEEAAPRAR ASERPARTFK
KKPAPRFIII AIDPGHGGED PGALGRSGTY EKDVTLAIAR KLKRRIDQEP NMRSVLVRDG
DYFIPLRTRV EKARRVRADL FVSIHADAFV RPHARGSSVF ALSERGATSE AARWLAKTEN
DADLIGGVNL DVPDPYLKQT LLDLSQTASI NDSLKLGRAV LDELGNVNTL HKPQVEQAGF
AVLKAPDIPS ILIETAFISN PQEERKLRNR AYQEKFAEAI FGGIKRYLAK NPPLARDKLV
LNP
//
