ID A0A1A7KL19_9FLAO Unreviewed; 341 AA.
AC A0A1A7KL19;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiD {ECO:0000313|EMBL:OBW42558.1};
GN ORFNames=AB670_01072 {ECO:0000313|EMBL:OBW42558.1};
OS Chryseobacterium sp. MOF25P.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1664318 {ECO:0000313|EMBL:OBW42558.1, ECO:0000313|Proteomes:UP000092708};
RN [1] {ECO:0000313|EMBL:OBW42558.1, ECO:0000313|Proteomes:UP000092708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOF25P {ECO:0000313|EMBL:OBW42558.1,
RC ECO:0000313|Proteomes:UP000092708};
RA David V.-J., Thomas B., Ramon P.Y., Thao N., David R., Richard E.,
RA Roderick C., Nikki M., Timothy W.J., Alexander A.E., Kimberley T.;
RT "A floR containing integrative conjugative element found in multidrug
RT resistant Chryseobacterium spp. isolates: exception to the general rule?";
RL Submitted (JUN-2015) 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:OBW42558.1}.
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DR EMBL; LFEG01000033; OBW42558.1; -; Genomic_DNA.
DR RefSeq; WP_066676598.1; NZ_LFEG01000033.1.
DR AlphaFoldDB; A0A1A7KL19; -.
DR PATRIC; fig|1664318.4.peg.1102; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000092708; Unassembled WGS sequence.
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 Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
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 Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OBW42558.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092708}.
FT DOMAIN 93..235
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 28..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 38549 MW; 1E03FA33F8C508E4 CRC64;
MRKTLYIISL STLVFSCTSQ KNIKKNTYRS KTPVSQPKTV TNSTSQEKIK PQITKESGVE
FFTTNIADIT KNDNTASYGS IVSAKPAGYK VVKTHFPAIA QNFRQKYLIL HYTVLPDDKS
ITVLTQQGVS AHYLVNNLGD NEIYQLVDEN KRSYHAGVSA WRADKNLNDT SIGIEIVNMG
FTADATGART FQPFSDDQIK KVAALAKDIV TRYNIPATNV LAHSDIAPLR KQDPGPQFPW
KKLYDEYQVG MWYDEATKQN LLTNAQTDVS TRYNESPFIF LVQTALQKFG YDISPNGKWD
DATKKTIEAL QYHFRPQNYN GIMDAETWAI LQALNQKYPT K
//
