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