ID K0YZ31_9ACTO Unreviewed; 285 AA.
AC K0YZ31;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=HMPREF9240_01846 {ECO:0000313|EMBL:EJZ84949.1};
OS Winkia neuii BV029A5.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Winkia.
OX NCBI_TaxID=888439 {ECO:0000313|EMBL:EJZ84949.1, ECO:0000313|Proteomes:UP000006075};
RN [1] {ECO:0000313|EMBL:EJZ84949.1, ECO:0000313|Proteomes:UP000006075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVS029A5 {ECO:0000313|EMBL:EJZ84949.1,
RC ECO:0000313|Proteomes:UP000006075};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces neuii subsp. anitratus BVS029A5.";
RL Submitted (JUL-2012) 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}.
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:EJZ84949.1}.
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DR EMBL; AGWP01000010; EJZ84949.1; -; Genomic_DNA.
DR RefSeq; WP_004808305.1; NZ_JH815218.1.
DR AlphaFoldDB; K0YZ31; -.
DR GeneID; 78951327; -.
DR PATRIC; fig|888439.3.peg.1854; -.
DR eggNOG; COG5632; Bacteria.
DR HOGENOM; CLU_1010587_0_0_11; -.
DR OrthoDB; 9758772at2; -.
DR Proteomes; UP000006075; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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; IPR036365; PGBD-like_sf.
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 SUPFAM; SSF47090; PGBD-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000006075}.
FT DOMAIN 11..146
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 285 AA; 31151 MW; 081652BA2A6611E6 CRC64;
MAYQDITCYD SPNYTPGRGG TQVNVIVIHW WNSPDRNPGF EGAIRTLCNP AVGTSAHCVA
EAGRVAWIVN AADTAWHAGD YSVNKRSIGI ECNPRMSSAD LETIAQLIAN IRRDYGWRIP
LAKHNDFYNT ACPGTYAGKL AWLDARAEDI RRGAPAKVTP KADPAPAPGK LAEDGILGVA
SWKKIQAHLR TPQDGTISDQ VAEKQEYYPA IMEADPCPAQ FGNGDDGSQA IRELQARLKQ
TQDGILGPTT IRAWQANLHQ TQDGYLGENT AQAIQHALNT KGWMW
//
