ID A0A095VUW5_9GAMM Unreviewed; 451 AA.
AC A0A095VUW5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=HRUBRA_00135 {ECO:0000313|EMBL:KGE05252.1};
OS Pseudohaliea rubra DSM 19751.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohaliea.
OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE05252.1, ECO:0000313|Proteomes:UP000029640};
RN [1] {ECO:0000313|EMBL:KGE05252.1, ECO:0000313|Proteomes:UP000029640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE05252.1,
RC ECO:0000313|Proteomes:UP000029640};
RX PubMed=25414506;
RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT 19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL Genome Announc. 2:e01208-14(2014).
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 -!- 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:KGE05252.1}.
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DR EMBL; AUVB01000005; KGE05252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095VUW5; -.
DR STRING; 1265313.HRUBRA_00135; -.
DR PATRIC; fig|1265313.6.peg.135; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_014322_2_3_6; -.
DR Proteomes; UP000029640; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KGE05252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029640};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..451
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001912763"
FT DOMAIN 405..448
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 451 AA; 48857 MW; C64EB82D50B79528 CRC64;
MQHSITAEHG RRPGRRGARC LVVLGALAAL LATAAAGAAT VTDVRLWRAP DHTRIVLDLD
APAEHRVIVL DSPRRVVLDV SGVVLRSTVE ALPLEGTPIT RVRAGVREGS DLRLVFDMKA
TVTPRSFALR ANAQAADRVV LDLYDEAPPS DAPRKVARSD GRRDVVVAID AGHGGEDPGA
LGPGRLREKD VVLAIAQELH AHFEREPGFR PTLIRSGDYY VSLRGRRDLA RKRQADLFVS
IHADAFTRKE ANGASVYALS TRGATSTTAR YLAESENAAD LIGGVRLADK DEMLAGVLAD
LSMTSTLDAS LNMGTTVLGE MDTVARLHKR QVEQAAFAVL KSPDIPSILV ETGFISNPAE
ARKLSTASYR RQMAAAIFRG LRGWWRDHPP PGTLLAWEKE NGLGRQYTIA RGDTLSGIAH
RFNVSVNELK SYNSLRGDRI MVGKTLKIPA S
//
