ID   ACSA2_NOVHA             Reviewed;        1596 AA.
AC   Q59167;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cellulose synthase 2;
DE   Includes:
DE     RecName: Full=Cellulose synthase catalytic subunit [UDP-forming];
DE              EC=2.4.1.12;
DE   Includes:
DE     RecName: Full=Cyclic di-GMP-binding domain;
DE     AltName: Full=Cellulose synthase 2 regulatory domain;
GN   Name=acsAII;
OS   Novacetimonas hansenii (Komagataeibacter hansenii).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Novacetimonas.
OX   NCBI_TaxID=436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23769 / NCIMB 8246;
RX   PubMed=7665515; DOI=10.1128/jb.177.18.5276-5283.1995;
RA   Saxena I.M., Brown R.M. Jr.;
RT   "Identification of a second cellulose synthase gene (acsAII) in Acetobacter
RT   xylinum.";
RL   J. Bacteriol. 177:5276-5283(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC         beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC         COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- DOMAIN: There are two conserved domains in the globular part of the
CC       catalytic subunit: the N-terminal domain (domain A) contains the
CC       conserved DXD motif and is possibly involved in catalysis and substrate
CC       binding. The C-terminal domain (domain B) contains the QXXRW motif and
CC       is present only in processive glycosyl transferases. It could be
CC       involved in the processivity function of the enzyme, possibly required
CC       for holding the growing glycan chain in the active site.
CC   -!- MISCELLANEOUS: It is not essential for cellulose production in this
CC       strain.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 2 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the AcsB/BcsB family.
CC       {ECO:0000305}.
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DR   EMBL; U15957; AAA85264.1; -; Genomic_DNA.
DR   PIR; T31338; T31338.
DR   RefSeq; WP_003621570.1; NZ_LUCI01000092.1.
DR   AlphaFoldDB; Q59167; -.
DR   SMR; Q59167; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003919; Cell_synth_A.
DR   InterPro; IPR003920; Cell_synth_B.
DR   InterPro; IPR018513; Cell_synthase_bac.
DR   InterPro; IPR005150; Cellulose_synth.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR009875; PilZ_domain.
DR   Pfam; PF03170; BcsB; 1.
DR   Pfam; PF03552; Cellulose_synt; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF07238; PilZ; 1.
DR   PRINTS; PR01440; CELLSNTHASEB.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03030; CelA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW   Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1596
FT                   /note="Cellulose synthase 2"
FT                   /id="PRO_0000059261"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1553..1573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          570..669
FT                   /note="PilZ"
FT   REGION          1..749
FT                   /note="Catalytic"
FT   REGION          145..238
FT                   /note="Catalytic subdomain A"
FT   REGION          315..375
FT                   /note="Catalytic subdomain B"
FT   REGION          750..1596
FT                   /note="Cyclic di-GMP binding domain"
FT                   /evidence="ECO:0000255"
FT   REGION          769..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..807
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000255"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1596 AA;  175801 MW;  D98A6F6259E1F3CE CRC64;
     MIYRAILKRL RLEQLARVPA VSAASPFVMM AVGVFLMLMA GGVTISTTSQ AFVTCGTVGL
     FLLLKGRKGR GVTCFLMMLS LLVSLRYMVW RLTTTLELHS PLQAALSLLL VAAELYALLT
     LCLSYFQMSW PLDRKPLPLP ADTTDWPVVD VYVPSYNEEL SLVRSTVLGA LAIDWPADKL
     NVYILDDGRR KSFHAFAMEA GAGYIIRDQN NHAKAGNLNH ALRVTEGEYV VIFDCDHIPT
     RGFLKKTIGW MMADPKLALL QTPHHFYSPD PFQRNLATGQ NVPPEGNMFY GLVQDGNDFW
     DATFFCGSCA AIRRSAVLGI GGFATETVTE DAHTALKMQR EGWHTAYLRQ PLAAGLSTER
     LMLHIGQRVR WARGMLQIMR LDNPLLGSGL RWQQRLCYLS AMSHFLFAIP RLVFLASPLA
     FLFLGQNIIA ASPFAILVYA FPHVFHSIGT LSRVEGRWRY SFWSEIYETT LALFLVRVTI
     MTLLNPRKGE FNVTDKGGLL QSEYFDLNAV YPNVILAVIL ALALVRGIGG MMWEYHDRLA
     LQSFALNTLW VAVSLIIVLA SIAVGRETRQ IRHKPRVRAT LPITLIDEHG QHYHAHTSDI
     SLGGIAARLS TEHALPTQTR VTMLYHNEKD GIDVRIPAVI LFSKPGQLHL QWSVDDLDVE
     RQIVEFMFGR NDAWSNWGDF QPDRPVRSFL MVLRSIGGLF RRGQRLFRWQ APQEAPLAES
     EHVEEEKLEK KSLVLKPVRR SARHGATASL IVLLGLPAAI APSLAQAPSR ATPVATEQGA
     TPVEPPPVNA PPPPSLPQPP GTLPTPPQIA PASAGELLPA ATAVSLPTGP ATQQMRERLS
     ERTGVSPASP FGDTNTGALP ADPSAPPIDP ADAARVADGE ITRTSTFRDL GLATGPLTLR
     GFSPLQGLDV IVPANRVVTR ARITLSGALS PSLLPEASAV SVTLNEQYVG TIRVDPEHPR
     FGPITFDIDP LYFTGDNKLN FHFAGEYRRD CNDLYNEVLW ARISDFSTVT LTTTRIAPDR
     KLSYLPAPFY DPNLRTPLRV PVVMPNPDAH GMLKASALVA SWFGKLADFR KVSFPVSTTI
     PASGNAIAIG ENLPIDARGT RPTGPTLSEV ENPNDRLGTI LVLTGRNAQE VEVAARVLAF
     SSDTLGAVGT KVVNDVTLQP RHPYDAPAFV PTDRPVRFGE LVAASDLQGG GFAPPVMALP
     FHLPPDLYSW RNRPYPIDLW VRTPGGPVVD LETSRLDVHL NNNYLDSFTL KPPSLWAAWS
     ERLVNQHAGA VEHAAALPPW LLFGQNQLKF SFDARPIDRG VCRRTPDDIH MSVDSDSWLD
     FRRGYHFARL PNLSYFAEAA FPFSRMADLS ETTVVVPHHI DAGTAGTFMD LMGFFGATTW
     YPASGVQVAD INDLSEHPPQ GDILILATAG DAPKFEELLT RAPYELTDGH IRVGQHMGLQ
     GIWYLFQDHD HAGLQDGVQA NLNAPIAGAG VLLGAQSPYR SDRSVVALMG DTPSRMHDLV
     MGLRSKEDVP RIQGDLVLRN GDRLTSYRTA PTFTMGSLPW WMWLDWYLGT RPLTLYVLGL
     VGAGLVAAAA VRLLRRRAQH RLEEAARVKD TTDASH