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Database: UniProt
Entry: A0R9C7_BACAH
LinkDB: A0R9C7_BACAH
Original site: A0R9C7_BACAH 
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
//
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