ID C9MSK6_9BACT Unreviewed; 426 AA.
AC C9MSK6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EEX17483.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:EEX17483.1};
GN ORFNames=HMPREF0973_02625 {ECO:0000313|EMBL:EEX17483.1};
OS Prevotella veroralis F0319.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=649761 {ECO:0000313|EMBL:EEX17483.1, ECO:0000313|Proteomes:UP000003327};
RN [1] {ECO:0000313|EMBL:EEX17483.1, ECO:0000313|Proteomes:UP000003327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0319 {ECO:0000313|EMBL:EEX17483.1,
RC ECO:0000313|Proteomes:UP000003327};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX17483.1}.
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DR EMBL; ACVA01000066; EEX17483.1; -; Genomic_DNA.
DR RefSeq; WP_004384311.1; NZ_GG698717.1.
DR AlphaFoldDB; C9MSK6; -.
DR STRING; 649761.HMPREF0973_02625; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_4_5_10; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000003327; 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; 3.40.630.40; Zn-dependent exopeptidases; 1.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EEX17483.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003327};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..426
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002999429"
FT DOMAIN 88..247
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 280..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 47695 MW; 1926EC0EEB3F3D6A CRC64;
MFKKITLFIV FFVLFVGTSW AANGRFTLVI DAGHGGHDAG ALGAISKEKD INLNVALAFG
RYVEQNLPDV QVIYTRKTDV FIPLHQRADI ANKAKADLFI SVHTNSVVPG HYAKGFQVYT
LGMHRAKDNL DVAMRENSVI SMEKGYQQTY QGFDPKSSES YIMFEFMQNA NMEKSVELAR
LIQRSVCSSA NRIDKGVHQA GFLVLRESYM PSCLIELGFI TAADEEEFLN SPDGIDAMAK
GIYNAFVKYK NMYDTHIVVP YKAADNRKIS VTRVVPVPPS GQPNLVSSNT MAQSTKKVPT
KKTIKEAPKK ETPVSSSNKT KTDAKKDNKV SAPINAPIFK VQVIASSRQL RPGCEQFKGH
KDIECIQEGS WYKYTIGNST NYNEIARLRE KLKKDFPQAF VIAYKAGNRM DTNDAINEFL
KNKRNK
//