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Database: UniProt
Entry: D1AY11_STRM9
LinkDB: D1AY11_STRM9
Original site: D1AY11_STRM9 
ID   D1AY11_STRM9            Unreviewed;       355 AA.
AC   D1AY11;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ACZ01187.1};
DE            EC=3.5.1.28 {ECO:0000313|EMBL:ACZ01187.1};
GN   OrderedLocusNames=Smon_0714 {ECO:0000313|EMBL:ACZ01187.1};
OS   Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS   9901).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Streptobacillus.
OX   NCBI_TaxID=519441 {ECO:0000313|EMBL:ACZ01187.1, ECO:0000313|Proteomes:UP000002072};
RN   [1] {ECO:0000313|EMBL:ACZ01187.1, ECO:0000313|Proteomes:UP000002072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901
RC   {ECO:0000313|Proteomes:UP000002072};
RX   PubMed=21304670; DOI=10.4056/sigs.48727;
RA   Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA   Del Rio T.G., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA   Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C.,
RA   Ovchinikova G., Pati A., Mavromatis K., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Sproer C., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Chain P.;
RT   "Complete genome sequence of Streptobacillus moniliformis type strain
RT   (9901T).";
RL   Stand. Genomic Sci. 1:300-307(2009).
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DR   EMBL; CP001779; ACZ01187.1; -; Genomic_DNA.
DR   RefSeq; WP_012858738.1; NC_013515.1.
DR   AlphaFoldDB; D1AY11; -.
DR   STRING; 519441.Smon_0714; -.
DR   GeneID; 29672939; -.
DR   KEGG; smf:Smon_0714; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_2_0_0; -.
DR   OrthoDB; 9772024at2; -.
DR   Proteomes; UP000002072; 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; 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:ACZ01187.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002072}.
FT   DOMAIN          201..350
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   355 AA;  40077 MW;  3FE1982C073E06BC CRC64;
     MLSKLKKILL LLTICFSTLT FSVILEDVRY QNGEFIIKFD SKITKPIINK TKITSNNIHY
     NVSEINLKNT KISEEVLNQI NINDEFYKYI IIDEITKDLA GIYTYSQYGY SSEITYSDDE
     IRIKKVKVDV PKKISPLTKK QLVIVLDAGH GGHDSGARGH GKLEKEIALE ITHKLARNLK
     RDHKVILTRS DDTFISLSER PAIGNNNFAD LFVSIHLNAA TNDNANGAEI FYFSKETNPY
     TSKLIESEEK YDEVQAKKVS IINQILGDFF VNRTKEKSAN LARVILDNYS KQMNFRKRGV
     FGANFAVLRG SESASILIEL GFISNESDNA KLASETGQMI AVNAIADAIR ENFEE
//
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