ID Q6HIJ0_BACHK Unreviewed; 410 AA.
AC Q6HIJ0;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase, family 3 {ECO:0000313|EMBL:AAT58922.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:AAT58922.1};
GN OrderedLocusNames=BT9727_2310 {ECO:0000313|EMBL:AAT58922.1};
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT58922.1, ECO:0000313|Proteomes:UP000001301};
RN [1] {ECO:0000313|EMBL:AAT58922.1, ECO:0000313|Proteomes:UP000001301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27 {ECO:0000313|EMBL:AAT58922.1,
RC ECO:0000313|Proteomes:UP000001301};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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DR EMBL; AE017355; AAT58922.1; -; Genomic_DNA.
DR RefSeq; WP_000791600.1; NC_005957.1.
DR RefSeq; YP_036636.1; NC_005957.1.
DR AlphaFoldDB; Q6HIJ0; -.
DR KEGG; btk:BT9727_2310; -.
DR PATRIC; fig|281309.8.peg.2445; -.
DR HOGENOM; CLU_029344_0_0_9; -.
DR Proteomes; UP000001301; 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 InterPro; IPR001119; SLH_dom.
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; PF00395; SLH; 3.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AAT58922.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..410
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004274119"
FT DOMAIN 23..82
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 83..146
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 147..207
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
SQ SEQUENCE 410 AA; 45233 MW; 9D55C07961CA3BF6 CRC64;
MKNKLIATGI LAGSLLSYST SIVADTHRFP DVPAWADKSV TYLVDKQVLS GYPDGTFGSS
DTLDRASAAT IMTKALGIHI DLNAKPSFKD SQNHWGTPYI AAAEKAGIIK GEGNGIFNPS
GKVTRAAMAT MLVNAYKLQN KNTSNGQSKF EDLKGHWGEK FANTLIDLKI SVGTDNGWQP
NKFITRAEAA QLTAKTDMLQ YSHSNPLENK TIIIDPGHGG EDPGKDTKGL PESKIVLDTS
LRLQKLLEKH TPFTVLLTRK SDTRPGHDQK SSLQERVKFA KQNQGDIFIS VHANAFNGNA
KGTETYYYKS SKSEKTNSHV EESRVLAEKI QNRLVDALQT RDRGVKHGDL HVIRENDMPA
VLTELAFIDN GIDYSKLSTE NGRQIAAEAI YEGILDYYEW KGNNVSEYRL
//
