ID   BCSB3_KOMXY             Reviewed;         804 AA.
AC   Q9WX62;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   02-JUN-2021, entry version 62.
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=bcsBI;
OS   Komagataeibacter xylinus (Gluconacetobacter xylinus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Komagataeibacter.
OX   NCBI_TaxID=28448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JCM 7664 / NBRC 13693;
RX   PubMed=10382968; DOI=10.1093/dnares/6.2.109;
RA   Umeda Y., Hirano A., Ishibashi M., Akiyama H., Onizuka T., Ikeuchi M.,
RA   Inoue Y.;
RT   "Cloning of cellulose synthase genes from Acetobacter xylinum JCM 7664:
RT   implication of a novel set of cellulose synthase genes.";
RL   DNA Res. 6:109-115(1999).
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; AB015802; BAA77586.1; -; Genomic_DNA.
DR   SMR; Q9WX62; -.
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   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR003920; Cell_synth_B.
DR   InterPro; IPR018513; Cell_synthase_bac.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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..804
FT                   /note="Cyclic di-GMP-binding protein"
FT                   /id="PRO_0000000267"
FT   TOPO_DOM        19..766
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        767..787
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        788..804
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          24..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   804 AA;  85511 MW;  1888ADD82EFC50A3 CRC64;
     MKMVSLIALL VFATGAQAAP IASKAPAHQP TGSDLPPLPA AAPVAPAAQP SAQAVDPASA
     APASDAGSAS NADAILDNAE NAAGVGTDVA TVHTYSLQEL GAQSALTMRG AAPLQGLQFG
     IPADQLVTSA RLVVSGAMSP NLQPDNSAVT ITLNEQYIGT LRPDPTHPAF GPLSFDINPI
     FFVSGNRLNF NFASGSKGCA DPTNGLQWAS VSEHSQLQIT TIPLPPRRQL ARLPQPFFDK
     TVRQKVVIPF VLAQTFDPEV LKASGIIASW FGQQTDFRGV NFPVFSTIPQ TGNAIVVGVA
     DELPAALGRP SVSGPTLMEV ANPSDPNGTV LLVTGRDRDE VITASKGIGF GSSALPVASR
     MDVAPIDVAP RLANDAPSFI PTSRPVRLGE LVPVSALQGE GYTPGVLSVP FRVSPDLYTW
     RDRPYKLNVR FRAPDGPILD VARSHLDVGI NNTYLQSYSL REQSSVVDQL LRRVGVGTQN
     AGVEQHTLTI PPWMVFGQDQ LQFYFDAAPL AQPGCRPGPS LIHMSVDPDS TIDLSNAYHI
     TRMPNLAYMA SAGYPFTTYA DLSRSAVVLP DHPNGTVVSA YLDLMGFMGA TTWYPVSGVD
     IVSADHVSDV ADRNLIVLST LSNSADVSAL LANSAYQISD GRLHMGLRST LSGVWNIFQD
     PMSVMSNTHP TEVETTLSGG VGAMVEAESP LASGRTVLAL LSGDGQGLDN LVQILGQRKN
     QAKVQGDLVL AHGDDLTSYR SSPLYTVGTV PLWLIPDWYM HNHPFRVIVV GLVGCLLVVA
     VLVRALFRHA MFRRRQLQEE RQKS
//