ID F5W0D4_9STRE Unreviewed; 556 AA.
AC F5W0D4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EGL86570.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:EGL86570.1};
GN ORFNames=HMPREF9967_1425 {ECO:0000313|EMBL:EGL86570.1};
OS Streptococcus infantis SK1076.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1005705 {ECO:0000313|EMBL:EGL86570.1, ECO:0000313|Proteomes:UP000010138};
RN [1] {ECO:0000313|EMBL:EGL86570.1, ECO:0000313|Proteomes:UP000010138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1076 {ECO:0000313|EMBL:EGL86570.1,
RC ECO:0000313|Proteomes:UP000010138};
RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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:EGL86570.1}.
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DR EMBL; AFNN01000014; EGL86570.1; -; Genomic_DNA.
DR RefSeq; WP_006150577.1; NZ_AFNN01000014.1.
DR AlphaFoldDB; F5W0D4; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR OrthoDB; 9763643at2; -.
DR Proteomes; UP000010138; 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; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 3.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
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; PF01473; Choline_bind_1; 4.
DR Pfam; PF19085; Choline_bind_2; 1.
DR Pfam; PF19127; Choline_bind_3; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51170; CW; 3.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EGL86570.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..556
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003329981"
FT REPEAT 105..124
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 164..183
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 223..242
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 420..550
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 25..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 62754 MW; C48CBFA588C08C80 CRC64;
MKKTLLASAI TLTYLGFATS SALAEENQAQ TTSAETTQQT TTANKVETKE PVPSTEASSS
IPTTSTTNPS KTSAKKEESK APEVKKEGWV FEGNIWRFYE ANKAAINWKK INGKWYYFDK
DGIMLSDTIY DGYILTSSGA MVDSGWGKIK DNWYYANPSG RIVKKDWKKV DGVWYYFDKD
GIMLSNTIFD GYIFTNSGAM AESAWVKQDG KWYYAQASGS LIKNKWDKIG GVWYYFNKDA
TMASNQWQGS FYLKSSGAMA EKEWIFDKNY DSWFYLKSGG AYAVREWIGS YYLKAGGYMA
KNEWIFDNYY NAWYYLEDSG VYVTGTRKID GKAHQFQSNG KWIGEVPVSR GFEKGKYTYT
VFLDPGHGGK DPGAVYYNTN EKDLTMQVYQ KLRKELQGLG YTVLSSRDSD VYVDFVTERS
KIANNTNSDI FISIHFNASG SPASNRSGIQ TYSYEEAAGY PSRINSYWHN HPDRISESNR
LAADIHSSLL AETGAKDAGL LQSSFAVLRE TDKPAVLLEL GYIDNFNENQ QIRSDAYQNR
LVAGIVKGIQ KYYAGK
//
