ID A0A162CUF6_9FLAO Unreviewed; 256 AA.
AC A0A162CUF6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=AWE51_02575 {ECO:0000313|EMBL:KZS42344.1};
OS Aquimarina aggregata.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS42344.1, ECO:0000313|Proteomes:UP000076715};
RN [1] {ECO:0000313|EMBL:KZS42344.1, ECO:0000313|Proteomes:UP000076715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS42344.1,
RC ECO:0000313|Proteomes:UP000076715};
RA Wang Y.;
RT "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL Submitted (JAN-2016) 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:KZS42344.1}.
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DR EMBL; LQRT01000002; KZS42344.1; -; Genomic_DNA.
DR RefSeq; WP_066309907.1; NZ_LQRT01000002.1.
DR AlphaFoldDB; A0A162CUF6; -.
DR STRING; 1642818.AWE51_02575; -.
DR OrthoDB; 2546654at2; -.
DR Proteomes; UP000076715; 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 Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
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 SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-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:UP000076715}.
FT DOMAIN 63..240
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|Pfam:PF01510"
SQ SEQUENCE 256 AA; 29030 MW; 5D720E1BCE7B337B CRC64;
MKASSIPAHE KSFLKNGRDS LEKQFILTPE SIATGDGGTM DYLDCVRENN DDSFYYKETV
TKNKIVLHFT AGYLKGDMAQ LTMPSNHVST PFVIARDGTI LKLWSSGFWS YHLGRGAVGG
NTIMSKQTIG IELSNIGFLR ENGPNLVSSY SDSDVYCSKQ DTRFYTKLNT PFRGEQYFAT
FTQNQYKSLA VLLKYLTNAY NIPREFLPPN RRYETLGKSE IENFNGIVSH VNFRKSGKWD
IGEAFDWDRL IDAVNN
//
