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BCSB2_KOMSB
ID   BCSB2_KOMSB             Reviewed;         802 AA.
AC   O82860;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Cyclic di-GMP-binding protein;
DE   AltName: Full=CDGBP;
DE   AltName: Full=Cellulose synthase regulatory subunit;
DE            Short=Cellulose synthase protein B;
DE   Flags: Precursor;
GN   Name=bcsB;
OS   Komagataeibacter sucrofermentans (strain ATCC 700178 / DSM 15973 / CECT
OS   7291 / JCM 9730 / LMG 18788 / BPR 2001) (Acetobacter xylinus subsp.
OS   sucrofermentans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Komagataeibacter.
OX   NCBI_TaxID=1307942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700178 / DSM 15973 / CECT 7291 / JCM 9730 / LMG 18788 / BPR
RC   2001;
RX   PubMed=9630539; DOI=10.1016/s0378-1119(98)00191-7;
RA   Nakai T., Moriya A., Tonouchi N., Tsuchida T., Yoshinaga F., Horinouchi S.,
RA   Sone Y., Mori H., Sakai F., Hayashi T.;
RT   "Control of expression by the cellulose synthase (bcsA) promoter region
RT   from Acetobacter xylinum BPR 2001.";
RL   Gene 213:93-100(1998).
CC   -!- FUNCTION: Binds the cellulose synthase activator, bis-(3'-5') cyclic
CC       diguanylic acid (c-di-GMP). {ECO:0000250}.
CC   -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC   -!- SUBUNIT: Tightly associated with the cellulose synthase catalytic
CC       subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AcsB/BcsB family. {ECO:0000305}.
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DR   EMBL; AB010645; BAA31464.1; -; Genomic_DNA.
DR   AlphaFoldDB; O82860; -.
DR   SMR; O82860; -.
DR   UniPathway; UPA00694; -.
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:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   InterPro; IPR003920; Cell_synth_B.
DR   InterPro; IPR018513; Cell_synthase_bac.
DR   PANTHER; PTHR39083; PTHR39083; 1.
DR   Pfam; PF03170; BcsB; 1.
DR   PRINTS; PR01440; CELLSNTHASEB.
PE   3: Inferred from homology;
KW   c-di-GMP; Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW   Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..802
FT                   /note="Cyclic di-GMP-binding protein"
FT                   /id="PRO_0000000266"
FT   TOPO_DOM        19..764
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        765..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        786..802
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          23..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..54
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   802 AA;  85306 MW;  8E8E52F89810EC10 CRC64;
     MKMVSLIALL VFATGAQAAP VASKAPAPQP AGSDLPPLPA APPQAAPPAA ASAAPPATTP
     AADASAASAA DAVVDNAENA IAGSDVATVH TYSLRELGAQ SALKMQGAAT LQGLQFGIPA
     DQLVTSARLV VSGAMSPSLQ PDTSAVTITL NEQFIGTLRP DPTHPTFGPL SFDINPIFFI
     SGNRLNFSFA SSSKGCTDPS NGLFWASVSE HSELQITTIP LPPHRQLSRL PQPFFDKNVK
     QKIVIPFVLA QTFDPEVLKA TGILASWFGQ QTDYRGVTFP VFSTIPQTGN AVVVGVADEL
     PSALGRQAVS GPTLMEVANP SDPNGTILLV TGRDRDEVIT ASKGIGFGSS TLPTANRMDV
     APIEVGARVA NDAPSFIPTN RPVRLGELVP DSALQAEGYA PGALAVPFRV SPDLYTWRDR
     PNKLNVRFRA PPGPIVDVSR SSLNVGINDT YLEAYPLREP DSPLDQLLHG VGLGHRNNDS
     VQQHTMPIPT YRVFGQNQLL FYFEMAAMVE PGCKPGPSTF HMGIDPNSTI DLSNSYHITQ
     MPNLAFMASA GFPFTTYADL SRSAVVLPEH PNGMIVSAYL DLMGFMGATT WYPVSGVDVV
     SSDHVNDVAD RNLIVLSTLA NSGDVSQLLS NSAYQISDGR LHMALRSTLS GVWNLFQDPM
     SAINSTAPTD VESTLTGGVA AMVEAESPLA SGRTVLALLS GDGQGLNNLV QILAQRKNQA
     KIQGDLVLAH GDDLTSYRSS PLYTVGTVPL WLKPDWYMHN HPSRVVVVGL FGCLLVVAVL
     MRALTKHALR RRRELQEERQ RT
 
 
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