ID S9R1E6_9RHOB Unreviewed; 482 AA.
AC S9R1E6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ruthe_01702 {ECO:0000313|EMBL:EPX85773.1};
OS Rubellimicrobium thermophilum DSM 16684.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX85773.1, ECO:0000313|Proteomes:UP000015346};
RN [1] {ECO:0000313|EMBL:EPX85773.1, ECO:0000313|Proteomes:UP000015346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX85773.1,
RC ECO:0000313|Proteomes:UP000015346};
RX PubMed=24501632; DOI=10.4056/sigs.4247911;
RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL Stand. Genomic Sci. 8:480-490(2013).
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:EPX85773.1}.
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DR EMBL; AOLV01000013; EPX85773.1; -; Genomic_DNA.
DR AlphaFoldDB; S9R1E6; -.
DR STRING; 1123069.ruthe_01702; -.
DR PATRIC; fig|1123069.3.peg.1670; -.
DR HOGENOM; CLU_014322_2_1_5; -.
DR Proteomes; UP000015346; 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; 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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EPX85773.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..482
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004555554"
FT DOMAIN 243..398
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 377..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 50937 MW; 836B1A9A1D19A175 CRC64;
MIGRIAALAM VLLLAMAQGA VSQAMSGLAR VDPQRSRVAD EGRGLAVDLA LSQAVPWRLF
TLDGPPRLVI DFAEADFGAI RPDALLMPGR AAGLRFGSVR PGWSRLVIDL ARPMGITQAG
MQVDEHDGTA RLRIRLDPVD AEAFAAAAGA PPDEEWGRAV LSPDRLADSP AAAAPAPSQD
GRFVVAIDPG HGGIDPGAER DGLRESHLML ALGIELAEAV ARAGMVPVLT RTEDVFVPLQ
TRMSIARAAG ADVLISLHAD ALETDQAQGA SVYTLTQEAA DAASERMVQR HEGGDLIAGL
DLTGTDDTVA TALLDLARRD TVPRSRRLAE TLAASLREAG AVVNGRALRQ AQLAVLSAAD
FPSVLLEAGF LSDEGDRARL SSPEGRAPHH CGHRRGAAGL ARGRGGTELP SAALNLHLRA
LSCAAEPARW SDPRRPPPRA RSPAPQNRLR PAGCGIRPGR DWHDRDRSGR CGRSRRRPSV
RS
//
