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Database: UniProt
Entry: A7GHX8_CLOBL
LinkDB: A7GHX8_CLOBL
Original site: A7GHX8_CLOBL 
ID   A7GHX8_CLOBL            Unreviewed;       962 AA.
AC   A7GHX8;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Putative N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ABS39357.1};
GN   OrderedLocusNames=CLI_3169 {ECO:0000313|EMBL:ABS39357.1};
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772 {ECO:0000313|EMBL:ABS39357.1, ECO:0000313|Proteomes:UP000002410};
RN   [1] {ECO:0000313|Proteomes:UP000002410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F
RC   {ECO:0000313|Proteomes:UP000002410};
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000728; ABS39357.1; -; Genomic_DNA.
DR   RefSeq; WP_012100818.1; NC_009699.1.
DR   AlphaFoldDB; A7GHX8; -.
DR   KEGG; cbf:CLI_3169; -.
DR   HOGENOM; CLU_011984_0_0_9; -.
DR   Proteomes; UP000002410; Chromosome.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR30032:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE CWLM; 1.
DR   PANTHER; PTHR30032; N-ACETYLMURAMOYL-L-ALANINE AMIDASE-RELATED; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF07495; Y_Y_Y; 5.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
FT   DOMAIN          824..957
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   962 AA;  108455 MW;  43E8761DBE0E5FD1 CRC64;
     MGKIFLLKER RGNIYMGEIE NIAKKIPIIL LISIIVAFVP SFKVHASSTT PIMGQHQLAQ
     EQALNYFRSR NSEKSDQDIK DFISIIWQEA NLEGIRADVV FMQIMKETNF LRFTGDVKEC
     QNNFAGIGAT GDGVAGAYFK DTRTGVRAVV QHLKAYCSTE GLKNPCVDPR FTYVQRGISP
     YVEWLGIGEN PNYPDKGWAA DNNYGKSIVE MMNSAKYLAN EGDSQGNITT SKATINNLEV
     SLDGNKMTTN ELEPGKSYNI KAYGNSSNGV LYEYWIKDLS INSWIKLKDY STSTQVTWTP
     NKPGKYLIGV HVKDKYSKEK LDNFKYVEYN VASLKKATIS SLEVSLDGNN VVNNELQLGK
     TYNIKAYGSS SNGVLYEYWI KDLSKNSWMK LRDYSTSTQV TWTSNKSGKY LLGVHVKDRY
     SEERLDNFKY VEYNVASPKK ATVNSLEVIL DGNKVVTNEL DPGKSYNIKV YGNSSNGVLY
     EYWIKDLSIN SWIKLKDYST STQVTWTPNK PGKYLIGVHV KDKYSKEKLD NFKYVDYNVT
     SPKKANINSL EVSLDGTKVV NNELQAGEIY NIKAYGSSFN GVLYEYWIKD LSINSWIKLK
     DYSTSTQVTW TPNKSGKYLI GVHVKDKYST QKLDNFKYVE YNVKLSKKAV ISNLEVSLNG
     KIVTNNQLNS GKTYSIKTYA ESLNGVLYEY WIKDLSSNSW IKLKDYSTST QITWTPNKAG
     KYLIGVHVKD KYSNERLDNH KYVEYSIQGD LIKTIVLDAG HGGKDSGAVS SKATGNVHEA
     DIVQKITIKL GNLLKKAGYN VIYTRDKVDN YNYPSITQNL EDRINVANSI KADLFMSIHA
     DSFDIPSANG YGAHYSSYRP NLDNSGVYKE GDVYYDRTPC DAALKSKVLS QLIVNEMSSL
     GGSNRGIEDH NLYVTRNALM PSVLVETGFV SNDTEVRKLN SDSYQNQIAQ KLYNAVTKLF
     SM
//
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