ID Q63GP9_BACCZ Unreviewed; 367 AA.
AC Q63GP9;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=Polysaccharide deacetylase-like protein {ECO:0000313|EMBL:AAU19936.1};
GN OrderedLocusNames=BCE33L0303 {ECO:0000313|EMBL:AAU19936.1};
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU19936.1, ECO:0000313|Proteomes:UP000002612};
RN [1] {ECO:0000313|Proteomes:UP000002612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
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).
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000256|ARBA:ARBA00010973}.
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DR EMBL; CP000001; AAU19936.1; -; Genomic_DNA.
DR RefSeq; WP_000761001.1; NZ_CP009968.1.
DR AlphaFoldDB; Q63GP9; -.
DR KEGG; bcz:BCE33L0303; -.
DR PATRIC; fig|288681.22.peg.5303; -.
DR OMA; RYTIWRT; -.
DR Proteomes; UP000002612; Chromosome.
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; cd10918; CE4_NodB_like_5s_6s; 1.
DR Gene3D; 2.60.40.3760; -; 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 PANTHER; PTHR34216; -; 1.
DR PANTHER; PTHR34216:SF3; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 205..367
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 367 AA; 42182 MW; 5B652DE26C030A09 CRC64;
MKKYTYIALL SSAILVGCNT SSTSDKQIQE TTAKQAVEQK KAKAVELPLT QGVITWDPYE
YNAQNTTIYT KDLRDSFKEV RYTIWRTADG PESKQTFTSQ EKERDFALPL HLKTFHLKRG
EFQIETVGIK EDNTETNLVT SKITFQQHVP VLMYHAIEKY PGPSDGDYGL YVPPEQFEKH
MQYLKDNGYT MLTFERWNDI NRVNKPIFIT MDDGRKNNMN ALHILQKLKD DTFQPAATEF
LTANEIDKPN RLSTDDIKQM MDSGIFSIQS HTANHTMMAH SNNYDEELRG SKEKIEALTG
KKVIALAYPV GSYNDPAVEE TKKYYEFAVT TDHGNHITKG MPNEQYLIKR HFVGPNTSME
KFLSLIK
//