ID A0R9C7_BACAH Unreviewed; 266 AA.
AC A0R9C7;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:ABK83820.1};
DE EC=3.5.1.- {ECO:0000313|EMBL:ABK83820.1};
GN OrderedLocusNames=BALH_0423 {ECO:0000313|EMBL:ABK83820.1};
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK83820.1, ECO:0000313|Proteomes:UP000000761};
RN [1] {ECO:0000313|EMBL:ABK83820.1, ECO:0000313|Proteomes:UP000000761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam {ECO:0000313|EMBL:ABK83820.1,
RC ECO:0000313|Proteomes:UP000000761};
RX PubMed=17337577; DOI=10.1128/JB.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA 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., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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DR EMBL; CP000485; ABK83820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0R9C7; -.
DR KEGG; btl:BALH_0423; -.
DR HOGENOM; CLU_021264_12_1_9; -.
DR OMA; GNHSYHH; -.
DR Proteomes; UP000000761; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10948; CE4_BsPdaA_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR014235; Spore_PdaA.
DR NCBIfam; TIGR02884; spore_pdaA; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR10587:SF78; PEPTIDOGLYCAN-N-ACETYLMURAMIC ACID DEACETYLASE PDAA; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABK83820.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..255
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 266 AA; 30767 MW; 179BE4D2DBAE3252 CRC64;
MERRLFMKYK WLYIGLIFSI MMALVPVSAL AYTNTPHNWG IPRPKNETVP DAGKLYTDLL
QKNGGFYLGD TKKKDIYLTF DNGYENGYTG KILDVLKEKK VPATFFVTGH YIKTQKDLLL
RMKDEGHIIG NHSWSHPDFT AVNDEKLREE LTSVTEEIKK VTGQKEVKYV RPPRGVFSER
TLALTKEMGY YNVFWSLAFL DWKVDEQRGW QYAHNNVMTM IHPGSILLLH AISKDNAEAL
AKIIDDLREK GYHFKSLDDL VKSNQP
//