ACSD_KOMXY
ID ACSD_KOMXY Reviewed; 156 AA.
AC P37719;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Cellulose synthase operon protein D;
GN Name=acsD;
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=ATCC 53582 / NQ5;
RX PubMed=8083166; DOI=10.1128/jb.176.18.5735-5752.1994;
RA Saxena I.M., Kudlicka K., Okuda K., Brown R.M. Jr.;
RT "Characterization of genes in the cellulose-synthesizing operon (acs
RT operon) of Acetobacter xylinum: implications for cellulose
RT crystallization.";
RL J. Bacteriol. 176:5735-5752(1994).
CC -!- FUNCTION: May have a major role in the perfection of crystallization,
CC involved either in the pore structure itself or in the organization of
CC the pores within the linear array of terminal synthesizing complexes
CC (TCs).
CC -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC -!- INTERACTION:
CC P37719; P37719: acsD; NbExp=3; IntAct=EBI-15882347, EBI-15882347;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X54676; CAA38490.1; -; Genomic_DNA.
DR PDB; 3A8E; X-ray; 3.00 A; A/B/C/D=1-156.
DR PDB; 3AJ1; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-156.
DR PDB; 3AJ2; X-ray; 2.80 A; A/B/C/D=1-156.
DR PDBsum; 3A8E; -.
DR PDBsum; 3AJ1; -.
DR PDBsum; 3AJ2; -.
DR AlphaFoldDB; P37719; -.
DR SMR; P37719; -.
DR DIP; DIP-59402N; -.
DR UniPathway; UPA00694; -.
DR EvolutionaryTrace; P37719; -.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.2590; -; 1.
DR InterPro; IPR022798; BcsD_bac.
DR InterPro; IPR038470; Cellsynth_D_sf.
DR Pfam; PF03500; Cellsynth_D; 1.
DR PRINTS; PR01442; CELLSNTHASED.
PE 1: Evidence at protein level;
KW 3D-structure; Cellulose biosynthesis.
FT CHAIN 1..156
FT /note="Cellulose synthase operon protein D"
FT /id="PRO_0000064442"
FT HELIX 11..41
FT /evidence="ECO:0007829|PDB:3AJ1"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3AJ1"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:3AJ1"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:3AJ1"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:3AJ1"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:3AJ1"
FT TURN 97..101
FT /evidence="ECO:0007829|PDB:3AJ1"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:3AJ1"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3AJ2"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3AJ2"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:3AJ1"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:3AJ1"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:3AJ1"
SQ SEQUENCE 156 AA; 17375 MW; A223BE2B7F801D6B CRC64;
MTIFEKKPDF TLFLQTLSWE IDDQVGIEVR NELLREVGRG MGTRIMPPPC QTVDKLQIEL
NALLALIGWG TVTLELLSED QSLRIVHENL PQVGSAGEPS GTWLAPVLEG LYGRWVTSQA
GAFGDYVVTR DVDAEDLNAV PRQTIIMYMR VRSSAT