ID C7D7A9_9RHOB Unreviewed; 400 AA.
AC C7D7A9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=TR2A62_1042 {ECO:0000313|EMBL:EET46332.1};
OS Thalassobium sp. R2A62.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassobium.
OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET46332.1, ECO:0000313|Proteomes:UP000004701};
RN [1] {ECO:0000313|EMBL:EET46332.1, ECO:0000313|Proteomes:UP000004701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R2A62 {ECO:0000313|EMBL:EET46332.1,
RC ECO:0000313|Proteomes:UP000004701};
RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAY-2009) 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};
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DR EMBL; GG697169; EET46332.1; -; Genomic_DNA.
DR AlphaFoldDB; C7D7A9; -.
DR STRING; 633131.TR2A62_1042; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_1_5; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000004701; 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 Reference proteome {ECO:0000313|Proteomes:UP000004701};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..400
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002977033"
FT DOMAIN 230..385
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 400 AA; 42964 MW; 4F72643534383487 CRC64;
MMILRAIFLW LPTAIPLMAQ DFSALARVDM SASQIIDTRR GLSVELALSQ VVPYRVYMLD
APTRLVLDFK EVDWTGVSEP ALLNADRATG LRYGSVETGW SRLVIALSTP LLIDTAGVVV
DQNTGTAQLS IDLAPTDPET FAANAGAPVD PTWGTPRFPA PPENPDGRLI VVLDPGHGGL
DPGAQRGGVK EADLMLTLAR EVEDALRRSG QIVPVLTRND DSFVSLDARR KLARAVGADV
LISLHADALT EGQATGATIY TLSDEASDLA SQQLATKLSR DDLLAGVDLT GRDDQVATIL
MDLARQETEP RTATLAEALV EGLGQQGVKL NSRPLRRAEI SVLKSPEIPS VLIEVGFLSN
DADLLALQDP ATRNRFVGGI LRGVLLWSIS EAKTDARRLR
//
