ID A0A1V4B3V5_9PAST Unreviewed; 423 AA.
AC A0A1V4B3V5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiB {ECO:0000313|EMBL:STO60485.1};
GN ORFNames=NCTC1659_01775 {ECO:0000313|EMBL:STO60485.1};
OS Canicola haemoglobinophilus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Canicola.
OX NCBI_TaxID=733 {ECO:0000313|EMBL:STO60485.1, ECO:0000313|Proteomes:UP000254329};
RN [1] {ECO:0000313|EMBL:STO60485.1, ECO:0000313|Proteomes:UP000254329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC1659 {ECO:0000313|EMBL:STO60485.1,
RC ECO:0000313|Proteomes:UP000254329};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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 -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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DR EMBL; UGHF01000001; STO60485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4B3V5; -.
DR STRING; 733.B0186_01325; -.
DR Proteomes; UP000254329; 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; 3.10.350.10; LysM domain; 2.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
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:SF6; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIB; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:STO60485.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254329};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..423
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030036312"
FT DOMAIN 286..329
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 377..421
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 333..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 47869 MW; 69EB9AD3377E9212 CRC64;
MNYLQRFISV ILALFAFSHA FANVWTIAID PGHGGKDPGA IGRNLNIYEK NVTLSIAREL
KKLLDKDPNF RAVLTRKGDY YISVPQRSEI ARKHKANYLV SIHADSSVST LLRGASVWVL
SNRRANSEMG QWLEDHEKRS ELLGGAGNVL ASHKEKYLDQ TVLDLQFGHS QRAGYELGSI
VLRHFARIAT LSRNTPQHAS LGVLRSPDIP SILVETGFLS NVEEEKKLNT LAYRKQLAKV
IYESLVEYRN RNFKAEFSSI KENHQPKQNK SAVDKTEEIQ IKDSGIRHKV KSGESLGGLA
AKYKVKTKDI ISLNKLKRNE LWIGETIKIP ENSKNSVQEK PQNSIKEKTT SKNKTEPKDK
SVAPVKNKEK TEDKSKKFHI VQKNQTLYAI SREYNIPVST LLKLNPKLKE GKVQTGQKIR
LHD
//
