ID A5I6J1_CLOBH Unreviewed; 949 AA.
AC A5I6J1;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:CAL84673.1};
GN OrderedLocusNames=CBO3110 {ECO:0000313|EMBL:CAL84673.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL84673.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL84673.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM412317; CAL84673.1; -; Genomic_DNA.
DR RefSeq; YP_001255602.1; NC_009495.1.
DR AlphaFoldDB; A5I6J1; -.
DR SMR; A5I6J1; -.
DR KEGG; cbo:CBO3110; -.
DR PATRIC; fig|413999.7.peg.3089; -.
DR HOGENOM; CLU_011984_0_0_9; -.
DR Proteomes; UP000001986; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT DOMAIN 811..944
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 949 AA; 106582 MW; 4D1D806D98B1925F CRC64;
MYMGEIENIV KKIPLILLIS IIVTFVPSFK VHASSTTHIM GQPQLTQEQA LNYFKTRNSE
KSDQATKEFI SIVWQEANLE GIRADVVFIQ IMKETNFLKF TGDVKECQNN FAGIGATGGG
VPGAYFKDTK TGVRAVVQHL KAYCSTEGLK NPCVDPRFTY VQRGISPYVE WLGIGENPNY
PDKGWAADNN YGKSIVEMMH SAKYLANEGD SQGNITTSKA TINNLEVSLD GNSVVTNELE
PGKAYNIKAY GNSSNGVLYE YWIKDLSINS WIKLRDYSTT NEVKWTPNKS GKYLIGVHVK
DRYSKERLDN FKYVEYNVAS LKKATISSLE VSLDGNNVVN NELQLGKIYN IKAYGSSSNG
VLYEYWIKDL SKNSWMKLRD YSTSTQVTWT PNKSGKYLLG VHVKDRYSEE RLDNFKYVEY
NVASPKKATV DSLEVSLDGN KVETNELDPG KAYNIKAYGN SSNGVLYEYW IKDLSINSWI
KLKDYSTSTQ VTWTPNKSGK YLIGVHVKDK YSTQKLDNFK YVEYNVASPK KATVNSLEVS
LNEGKVVNNE LQAGEIYNIK AYGSSSNGVL YEYWIKDLSI NSWIKLKDYS TSTQVTWTPN
KSGKYLIGVH VKDKYSAQKL DNFKYVEYNV KLSKKAVISN LEVSLNGNIV ANNQLNSGKT
YSIKAYAESL NGVLYEYWIK DLSSNSWIKL KDYSTSAQIT WTPNKAGKYL IGVHVKDKYS
NERLDNYKYV EYSVQGGLIK TIVLDAGHGG KDSGAVSSRA TGNIHEADIV QKITIKLGNL
LKKAGYNVIY TRDKVDNYNY TSVTQNLEDR INVANSINAD LFMSIHADSF DIPSANGYSA
HYSSYRPKLD NSGVYIEDDV YYDRTPCDAA LKSKVLSQLI VNEMSSLGGS NRGISDHNLY
VTKNALMPSV LVECGFVSND AEVRKLNGDT YQNQIAQKLY NAVTKLFSM
//
