ID A0A2C7AH15_9PROT Unreviewed; 383 AA.
AC A0A2C7AH15;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=CR162_05255 {ECO:0000313|EMBL:PHK96007.1};
OS Pseudoroseomonas rhizosphaerae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=1335062 {ECO:0000313|EMBL:PHK96007.1, ECO:0000313|Proteomes:UP000223527};
RN [1] {ECO:0000313|EMBL:PHK96007.1, ECO:0000313|Proteomes:UP000223527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YW11 {ECO:0000313|EMBL:PHK96007.1,
RC ECO:0000313|Proteomes:UP000223527};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-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};
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:PHK96007.1}.
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DR EMBL; PDNU01000005; PHK96007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C7AH15; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000223527; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PHK96007.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000223527};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..383
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013061694"
FT DOMAIN 217..369
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 383 AA; 40184 MW; E2F4CFCCE4570CDA CRC64;
MSDSPGRRQL LQMALGLAFA GLPAPAEAAV TAARLVRADG GSRLTIDVNG ATRWSLRATT
RPARLVLSLP GSSWRGPARL AGAGLVRGAR WDNANKRLLI DLAGPVSVAE ARAEGRQLAI
HIAPGTQPGF AQLARGTIAE GRFGATATAS GSSLPLVVLD PGHGGKDPGT IGAAGTLEKR
ITLAAALELK RQLEAGGRCR VALTRGRDVF VSLDGRVEFA RKRQAALFVS LHADSAPGAR
GASVYTLSDR ASDSLSARLA QSQNRADAAG GLRLPDVSPE VERILYSLVR QETKVGSARM
ARFVVDALGR SVPLLPNTHR QASFAVLKAP DVPSVLVEMG FLSDRRDEAA LNRAAHRALL
ARSMTRAIHG WLAQHHAGMA HAG
//
