ID A0A1W6Z2L9_9BORD Unreviewed; 460 AA.
AC A0A1W6Z2L9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=CAL13_16305 {ECO:0000313|EMBL:ARP87590.1};
OS Bordetella genomosp. 9.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416803 {ECO:0000313|EMBL:ARP87590.1, ECO:0000313|Proteomes:UP000194139};
RN [1] {ECO:0000313|EMBL:ARP87590.1, ECO:0000313|Proteomes:UP000194139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU17164 {ECO:0000313|EMBL:ARP87590.1,
RC ECO:0000313|Proteomes:UP000194139};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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};
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DR EMBL; CP021109; ARP87590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6Z2L9; -.
DR Proteomes; UP000194139; Chromosome.
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; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR006311; TAT_signal.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000194139}.
FT DOMAIN 289..444
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 181..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 50165 MW; 79227DEC65098F51 CRC64;
MAERDCPPPG VPRSRGAMSR RRLIGAAATL LVLPVIPRLA QAATILAVRT WPADEYTRVT
LELDSELKAE QFTLENPDRL VVDIEGLSMS ASLNDLAAKI RDGDPYIRSL RIAQNRPNVV
RLVFDLKQPV APQIFTLKPV ADYQYRLVLD LYPKIAQDPL LAILKKPPPP DVDDPLARIL
EDISRNPPGP NTATIPSSPT PLPSPQPPAV ALPRPSDTPK LGRKRMLTIA LDPGHGGEDP
GASGRTGLRE KDVVLRIAHR LKALIDAQPN MRAYLTRDDD YFVPLHVRVQ KARRVRADLF
VSIHADAWIK PTASGSSVFA LSQRGASSAA ARWLANKENA ADLIGGVNLG AHDEQVAKVL
LDLSTTAQIH DSLKLGTVLL EEIKKINRLH KDSVEQAGFA VLKAPDIPSI LVETAFISNP
NEEALLKSSS HQDKLAMAMF TGIQRYLTTN PPLARVGDVS
//
