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Database: UniProt
Entry: A0A1H2D0D2_9ACTN
LinkDB: A0A1H2D0D2_9ACTN
Original site: A0A1H2D0D2_9ACTN 
ID   A0A1H2D0D2_9ACTN        Unreviewed;       743 AA.
AC   A0A1H2D0D2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase {ECO:0000313|EMBL:SDT76238.1};
GN   ORFNames=SAMN04489716_7558 {ECO:0000313|EMBL:SDT76238.1};
OS   Actinoplanes derwentensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT76238.1, ECO:0000313|Proteomes:UP000198688};
RN   [1] {ECO:0000313|EMBL:SDT76238.1, ECO:0000313|Proteomes:UP000198688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT76238.1,
RC   ECO:0000313|Proteomes:UP000198688};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT629758; SDT76238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2D0D2; -.
DR   STRING; 113562.SAMN04489716_7558; -.
DR   OrthoDB; 3864432at2; -.
DR   Proteomes; UP000198688; Chromosome i.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:UP000198688};
KW   Transferase {ECO:0000313|EMBL:SDT76238.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        313..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        607..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        639..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..265
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          714..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   743 AA;  81065 MW;  6AA5EF74E8DB80BD CRC64;
     MIARRRVLPR PRVLLGVLLA ASFLSVLVVQ AYINAEFTGD HVESEVGDQA AVPPAILDGG
     PIINTTGGQE STSRLPDRTI ALTFDDGPDP AWTPKILDVL RRHDAHATFF VVGSQVARHP
     TIAKEIVTGG NELGLHTFTH PNMQRLAPWR RELELSQTQM AIAKATGART HLARFPYSSK
     NAAIDEVNWR LVQEAGALGY LVVVNDTDSE DWKRPGVEKI IQNATPAGDR SAVMLFHDAG
     GDRSQTVAAL DEFIPRMKAR GYRFTTVTEG LNLTIAGQAA KTHSPLPLNP AAPGSDKWRG
     TALIWTVNLA DGLVALIAGL FLVVGTLTVG RTLLLLVLAT RNARQRRSPA WTWGPPVTEP
     VSVIVPAYNE KEGIEAAVRS LAGGDHTRIE VVVVDDGSTD GTADLVDRMR LPNVRVVRVP
     NGGKPNALNT GVALARHDLI VMVDGDTVFE PDSLRLLVQP FADPTVGAVA GNVKVGNRET
     TVALWQHIEY VIGFNLDRRL YEVMNCMPTV PGAIGAFRRT ALAQVGGVSD ETLAEDTDVT
     MAMCRAGWRV VYEEKARAWT EAPTTMEQLY RQRYRWSYGT MQAMWKHRGA LLDSGPSGRF
     GRVGLPFLAL FGLALPMLAP VVDIMLVYGL VFWELGETVA AWFGMLALQL FTAAVAFRLD
     RESYRPLLRL PLQQFAYRQL MYLVLLQSAT TALTGGRLRW HKLNRAGLAP RSPALDRTAA
     DRGRVPVTPI TPSRGPLTPP PGP
//
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