ID I3ZXT5_ORNRL Unreviewed; 303 AA.
AC I3ZXT5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Ornrh_0301 {ECO:0000313|EMBL:AFL96519.1};
OS Ornithobacterium rhinotracheale (strain ATCC 51463 / DSM 15997 / CCUG 23171
OS / CIP 104009 / LMG 9086).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Ornithobacterium.
OX NCBI_TaxID=867902 {ECO:0000313|EMBL:AFL96519.1, ECO:0000313|Proteomes:UP000006051};
RN [1] {ECO:0000313|EMBL:AFL96519.1, ECO:0000313|Proteomes:UP000006051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51463 / DSM 15997 / CCUG 23171 / LMG 9086
RC {ECO:0000313|Proteomes:UP000006051};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Teshima H., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Lang E., Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Ornithobacterium rhinotracheale DSM 15997.";
RL Submitted (JUN-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}.
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DR EMBL; CP003283; AFL96519.1; -; Genomic_DNA.
DR RefSeq; WP_014790149.1; NC_018016.1.
DR AlphaFoldDB; I3ZXT5; -.
DR STRING; 867902.Ornrh_0301; -.
DR GeneID; 71568578; -.
DR KEGG; orh:Ornrh_0301; -.
DR PATRIC; fig|867902.3.peg.303; -.
DR eggNOG; COG3023; Bacteria.
DR HOGENOM; CLU_049290_2_1_10; -.
DR Proteomes; UP000006051; Chromosome.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006051}.
FT DOMAIN 63..200
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 303 AA; 35013 MW; C553FCA71492CCC9 CRC64;
MKNYWKKSLF ILGALSIVSC TTTKHVKVVK TITKTDTIYV NPFKDVDVNN YVVAKPEGYT
INNDYYPAVS QDFRQKFLIL HYTALDTPKS LMVLSERNVS VHYVVNDYDD NQINALVSEN
KRAWHAGVSY WGGRTNLNDS SIGIEIVNMG NTYGEYQDFP DYQIKKVGAL AKDIVSRYNI
DPTHVLGHED IAPQRKPDPG PKFPWKRLYD EYGVGAWYDE PTKIFYMNQF PEAQKDDMNF
IADFQKDLAT YGYEISPLGY WDEKSKKVVK AFQKHFRPTN YDGNLDAETW AILKALLKKY
KSK
//
