ID G2NKX2_STREK Unreviewed; 738 AA.
AC G2NKX2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Polysaccharide deacetylase {ECO:0000313|EMBL:AEN10327.1};
DE Flags: Precursor;
GN ORFNames=SACTE_2439 {ECO:0000313|EMBL:AEN10327.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN10327.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN10327.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN10327.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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DR EMBL; CP002993; AEN10327.1; -; Genomic_DNA.
DR AlphaFoldDB; G2NKX2; -.
DR STRING; 862751.SACTE_2439; -.
DR KEGG; ssx:SACTE_2439; -.
DR PATRIC; fig|862751.12.peg.2536; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_012505_0_0_11; -.
DR OrthoDB; 9763050at2; -.
DR Proteomes; UP000001397; 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; cd06423; CESA_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; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43630; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR PANTHER; PTHR43630:SF1; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR Pfam; PF13641; Glyco_tranf_2_3; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 320..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 643..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..281
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 82174 MW; C05F2FABEFF01624 CRC64;
MTTPAPRGRH NPRKKKRTTR RRLPMRYLLP SLLLVALLAM LMLRGYVHSE ILADHRVQPP
ASTSHVPDEV LDGGPVIDAR TPGERAKTLR IPDHKIVLTF DDGPDPVWTP KVLDQLKKYD
AHGVFFVTGT MASRYPALVQ RMVDEGHEVG LHTFNHPDLS YQSTGRIDWE LSQNQLVLAG
AAGIRTSLFR PPYSSFSDAM DNKSWPVTQY IGSRGYLTVV NDTDSEDWKR PGVRAIIDQA
TPRHGKGAVI LMHDSGGDRS QTVAALDKFL PRMQDRGYEF TNLTAALGAP SAHTPATGFA
LWKGKAFVYA VDISEHVTSV LVVGLAVIGV LVITRFGLML LLSFLHARRV RRKGFRWGEP
FTRPVSVLVP AYNERKCIES TVRSLVASDY PIEVVVIDDG STDGTADVVE AMGIPNVRVV
RQRNAGKPAA LNNGIAHARY DVVVMMDGDT VFEPTTVREL VQPFGDHRVG AVAGNAKVGN
RDSLIGAWQH IEYVMGFNLD RRMYDILGCM PTIPGAVGAF RRDALDRIGG MSEDTLAEDT
DVTMALHRDG WRVVYAENAR AWTEAPESVQ QLWSQRYRWS YGTMQAIWKH RRAVVERGPS
GRFGRVGLPF VSLFMVVAPL LAPLIDVFLL YGLVFGPTGK TVTAWFGVLL IQAVCAAYAF
RLDRERMTHL ISLPLQQILY RQLMYVVLLQ SWITALTGGR LRWQKLRRTG VVEAPGGAQA
RPVSRRKDPQ QTDRRPVA
//