ID A0A101RYU1_9ACTN Unreviewed; 199 AA.
AC A0A101RYU1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=cwhA_2 {ECO:0000313|EMBL:AYC43077.1};
GN ORFNames=AQJ54_24450 {ECO:0000313|EMBL:KUN64187.1}, DWG14_07383
GN {ECO:0000313|EMBL:AYC43077.1};
OS Streptomyces griseorubiginosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67304 {ECO:0000313|EMBL:KUN64187.1, ECO:0000313|Proteomes:UP000054375};
RN [1] {ECO:0000313|EMBL:KUN64187.1, ECO:0000313|Proteomes:UP000054375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40469 {ECO:0000313|EMBL:KUN64187.1,
RC ECO:0000313|Proteomes:UP000054375};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseorubiginosus DSM 40469, type
RT strain for the species Streptomyces griseorubiginosus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AYC43077.1, ECO:0000313|Proteomes:UP000265765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3E-1 {ECO:0000313|EMBL:AYC43077.1,
RC ECO:0000313|Proteomes:UP000265765};
RA Kang H.J., Kim S.B.;
RT "Production of Trimethoprim by Streptomyces sp. 3E-1.";
RL Submitted (SEP-2018) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CP032427; AYC43077.1; -; Genomic_DNA.
DR EMBL; LMWV01000020; KUN64187.1; -; Genomic_DNA.
DR RefSeq; WP_062240953.1; NZ_KQ948738.1.
DR AlphaFoldDB; A0A101RYU1; -.
DR KEGG; sge:DWG14_07383; -.
DR OrthoDB; 66275at2; -.
DR Proteomes; UP000054375; Unassembled WGS sequence.
DR Proteomes; UP000265765; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AYC43077.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054375}.
FT DOMAIN 51..184
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 199 AA; 22536 MW; C29AFBC106798E60 CRC64;
MERARPLFDR RRLLKGALLA AVPYTLLPET RAGAAPQSGD YPLAEWQPAT SSNFTESDRP
WSYRVNLVVV HVTQTTYTEA LDIFRNPAKQ VSAHYVVRSA DGHVAQCVRE ADVAWHAGNW
DYNTRSIGIE HEGWVDKPAY FTDALYEESA KLTAGICDKY GIPRDRAHII GHYEVPGSDH
TDPGPSWDWT RYMRMVEAM
//
