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Database: UniProt
Entry: A0A1I6LAQ5_9GAMM
LinkDB: A0A1I6LAQ5_9GAMM
Original site: A0A1I6LAQ5_9GAMM 
ID   A0A1I6LAQ5_9GAMM        Unreviewed;      1174 AA.
AC   A0A1I6LAQ5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase {ECO:0000313|EMBL:SFS00509.1};
GN   ORFNames=SAMN05216570_1436 {ECO:0000313|EMBL:SFS00509.1};
OS   Dyella sp. OK004.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1855292 {ECO:0000313|EMBL:SFS00509.1, ECO:0000313|Proteomes:UP000198834};
RN   [1] {ECO:0000313|EMBL:SFS00509.1, ECO:0000313|Proteomes:UP000198834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK004 {ECO:0000313|EMBL:SFS00509.1,
RC   ECO:0000313|Proteomes:UP000198834};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOZI01000002; SFS00509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6LAQ5; -.
DR   STRING; 1855292.SAMN05216570_1436; -.
DR   OrthoDB; 276604at2; -.
DR   Proteomes; UP000198834; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd06423; CESA_like; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PF00704; Glyco_hydro_18; 1.
DR   Pfam; PF13641; Glyco_tranf_2_3; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS51910; GH18_2; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198834};
KW   Transferase {ECO:0000313|EMBL:SFS00509.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1010..1031
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1052..1073
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1095..1115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..415
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          482..675
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   1174 AA;  130551 MW;  55D73FADE8A9C2B6 CRC64;
     MERKLVFVDP SGRRARRLSR VGRICAAIAA LSLAAFVTSL CLGPYVPPLQ LRERDMPYRR
     ESATPSIPKN DAARPEPMLS HVVNLVDPHV TTATASSPTT GRPLVAGFYT VFTKDDETAY
     RGLSHALPQL DWLMPTWLRM QGADMALQTS VDAKVVSLIH REKPDLSVLP TLQNISGRHW
     DGPGLARALA DPTIRRERIA QIVSFLTSNQ FQGVTVDFEG VPEDAHDDLR RFLAELSASM
     TPHHLRLVLA VPFDDDDWDY ADYAKVVDFE LLMAYDEHTE ADRIPGSVAG MPWYDEILRR
     RMSELDPRHT IVAIGSYGYD WSVEHGSKPV TFEETMVRAG QSDATINFDK TAQNPHFAYS
     ESDGSRHQVW FLDGVTAYNQ VRHADAYRPF AYGVWRIGSE DPSIWTVMRH EYGAPANPRL
     RQIDGGVNVQ MLGDGEILRV ASIPTTGSRA LRVNTVNGGI EDEHYDVLPQ PYAIQRVAGA
     PGNVAITFDD GPDVRWTPRV LDILKAKKAS ATFFVIGQNM QASPSLVQRM VNEGHEVGNH
     TFSHRGYAEG HGLAMWWQLA STQRLFEALT GRSMRLFRPP YLGNAEPTTS DELTPMEQAQ
     SLGYLTVGLH VDSDDWEELP PTLIVKRIME QLSSATSDRH AQVILMHDGG GDRSRTVAAL
     PLLIDTLRAK GYRLVTSSNI AGLSRDQSMP QLTGGTWPLK FIRAGFLGVE QTGSVLHWLL
     RLAIFLGIGR VVLLCGLALV DRIRESRRSP PTMENGDALV SVIIPAYNEE KVVLDCISHV
     LNSDYATLEV IVVDDGSTDA TAARIRRHFA HDARVVLMSR PNAGKAHALN AGLHFAKGEV
     LVALDADTQF ECNTISCLVR WFGDALVGAV AGNAKVGNRT NVITQWQALE YIVTQNLERR
     ALAALGTLTV VPGAVGAWRR SVLNELGGFP CDTLAEDQDL TIAVQKAGYR ALFDSEAIAW
     TEVPDRMGAL IRQRIRWSFG TLQCLWKHRD ALFRKSQGAL GLVALPQMWV FQYGLALLAP
     LVDVLLLWQI VNAAVDYTSH RDQFDSQGLS EIMLFYGVFL ATDMLAGGIA FALEKREQWH
     LLLWLVVQRF CYRQLLYFVT IRSIAAAWSG SLIAWGRQQR SATVRLTGLS HETDSSGYRL
     ARANRPERTR WSSAVLKRDT THLHKTRSSI ARFP
//
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