ID Q213N5_RHOPB Unreviewed; 431 AA.
AC Q213N5;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=RPC_2853 {ECO:0000313|EMBL:ABD88401.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD88401.1};
RN [1] {ECO:0000313|EMBL:ABD88401.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD88401.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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; CP000301; ABD88401.1; -; Genomic_DNA.
DR AlphaFoldDB; Q213N5; -.
DR STRING; 316056.RPC_2853; -.
DR KEGG; rpc:RPC_2853; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_1_5; -.
DR OrthoDB; 9806267at2; -.
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 Hydrolase {ECO:0000313|EMBL:ABD88401.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..431
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004199526"
FT DOMAIN 261..417
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 431 AA; 45389 MW; 1FD22C5163A4D041 CRC64;
MPGSANHKFV LGALVACAAA LLCLGAAAAG SAPAESPASA VSLFPVVSDA RLAGDAKQTR
FIVDLDSKLQ HRVFTLADPY RVVVDIPQVI FRLPAGAGTS GRGLVKAFRY GLVMPGGSRI
VLELNGPAKI ESTYVLDAAN GQPPRLVIEL AAVDRTAFVQ SLDAESRPEL RPAVGSVDAV
ASVTAAARPA VVTPLDSRPV VVLDPGHGGI DNGTQAASGE AEKTLVLDFA LALRDRIEKA
GKYRVVMTRT DDTFIPLGER VRIARAQSAA LFVSIHADAL PRGEGDAQGA TIYTLSDRAS
DAEAERLAES ENKADAIGGV NLTEEPTDVA DILIDLAQRE TKGFSNRFAR ILMTEMKSAA
RMHKHPLKSA GFKVLKAPDV PSVLLELGYV SNKGDLKQLV SENWRTRTVG SVAQAVDAFF
AKRVVSVGAP D
//
