ACSA1_KOMXY
ID ACSA1_KOMXY Reviewed; 1550 AA.
AC P0CW87; P21877; P37717;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Cellulose synthase 1;
DE Includes:
DE RecName: Full=Cellulose synthase catalytic domain [UDP-forming];
DE EC=2.4.1.12;
DE Includes:
DE RecName: Full=Cyclic di-GMP-binding domain;
DE AltName: Full=Cellulose synthase 1 regulatory domain;
GN Name=acsAB; Synonyms=acsA, acsB;
OS Komagataeibacter xylinus (Gluconacetobacter xylinus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=28448;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 6-20.
RC STRAIN=ATCC 53582 / NQ5;
RX PubMed=2151718; DOI=10.1007/bf00016118;
RA Saxena I.M., Lin F.C., Brown R.M. Jr.;
RT "Cloning and sequencing of the cellulose synthase catalytic subunit gene of
RT Acetobacter xylinum.";
RL Plant Mol. Biol. 15:673-683(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 768-781.
RC STRAIN=ATCC 53582 / NQ5;
RX PubMed=1830823; DOI=10.1007/bf00016067;
RA Saxena I.M., Lin F.C., Brown R.M. Jr.;
RT "Identification of a new gene in an operon for cellulose biosynthesis in
RT Acetobacter xylinum.";
RL Plant Mol. Biol. 16:947-954(1991).
RN [3]
RP SEQUENCE REVISION.
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).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 53582 / NQ5;
RX PubMed=2138620; DOI=10.1016/s0021-9258(19)34039-6;
RA Lin F.C., Brown R.M. Jr., Drake R.R. Jr., Haley B.E.;
RT "Identification of the uridine 5'-diphosphoglucose (UDP-Glc) binding
RT subunit of cellulose synthase in Acetobacter xylinum using the
RT photoaffinity probe 5-azido-UDP-Glc.";
RL J. Biol. Chem. 265:4782-4784(1990).
RN [5]
RP REVIEW ON DOMAIN ARCHITECTURE.
RX PubMed=7883697; DOI=10.1128/jb.177.6.1419-1424.1995;
RA Saxena I.M., Brown R.M. Jr., Fevre M., Geremia R.A., Henrissat B.;
RT "Multidomain architecture of beta-glycosyl transferases: implications for
RT mechanism of action.";
RL J. Bacteriol. 177:1419-1424(1995).
CC -!- FUNCTION: Bifunctional protein comprised of a catalytic subunit and a
CC regulatory subunit. The catalytic subunit of cellulose synthase
CC polymerizes uridine 5'-diphosphate glucose to cellulose in a processive
CC way. The thick cellulosic mats generated by this enzyme probably
CC provide a specialized protective environment to the bacterium. The
CC regulatory subunit binds bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
CC {ECO:0000269|PubMed:2138620}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by c-di-GMP.
CC {ECO:0000269|PubMed:2138620}.
CC -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Cellulose is produced at a linear rate with respect to cell
CC growth when O(2) is present.
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 -!- 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}.
CC -!- CAUTION: Was originally proposed to code for two separate adjacent
CC ORFs, ascA and ascB. {ECO:0000305|PubMed:2151718}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA38487.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA38488.1; Type=Frameshift; Evidence={ECO:0000305};
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; CAA38487.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X54676; CAA38488.1; ALT_FRAME; Genomic_DNA.
DR PIR; S13732; C36963.
DR PIR; S16266; S16266.
DR PDB; 4I86; X-ray; 2.10 A; A/B=572-670.
DR PDBsum; 4I86; -.
DR AlphaFoldDB; P0CW87; -.
DR SMR; P0CW87; -.
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: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; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009875; PilZ_domain.
DR Pfam; PF03170; BcsB; 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 1: Evidence at protein level;
KW 3D-structure; c-di-GMP; Cell inner membrane; Cell membrane;
KW Cellulose biosynthesis; Direct protein sequencing; Glycosyltransferase;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1550
FT /note="Cellulose synthase 1"
FT /id="PRO_0000059260"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1513..1533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 572..647
FT /note="PilZ"
FT REGION 1..741
FT /note="Catalytic"
FT REGION 147..240
FT /note="Catalytic subdomain A"
FT REGION 317..377
FT /note="Catalytic subdomain B"
FT REGION 711..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..1550
FT /note="Cyclic di-GMP binding domain"
FT REGION 768..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /evidence="ECO:0000255"
FT ACT_SITE 333
FT /evidence="ECO:0000255"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT STRAND 584..589
FT /evidence="ECO:0007829|PDB:4I86"
FT STRAND 595..603
FT /evidence="ECO:0007829|PDB:4I86"
FT STRAND 605..611
FT /evidence="ECO:0007829|PDB:4I86"
FT STRAND 622..630
FT /evidence="ECO:0007829|PDB:4I86"
FT STRAND 633..644
FT /evidence="ECO:0007829|PDB:4I86"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:4I86"
FT HELIX 658..670
FT /evidence="ECO:0007829|PDB:4I86"
SQ SEQUENCE 1550 AA; 168162 MW; 63AB8952BC39E961 CRC64;
MPEVRSSTQS ESGMSQWMGK ILSIRGAGLT IGVFGLCALI AATSVTLPPE QQLIVAFVCV
VIFFIVGHKP SRRSQIFLEV LSGLVSLRYL TWRLTETLSF DTWLQGLLGT MLLVAELYAL
MMLFLSYFQT IAPLHRAPLP LPPNPDEWPT VDIFVPTYNE ELSIVRLTVL GSLGIDWPPE
KVRVHILDDG RRPEFAAFAA ECGANYIARP TNEHAKAGNL NYAIGHTDGD YILIFDCDHV
PTRAFLQLTM GWMVEDPKIA LMQTPHHFYS PDPFQRNLSA GYRTPPEGNL FYGVVQDGND
FWDATFFCGS CAILRRTAIE QIGGFATQTV TEDAHTALKM QRLGWSTAYL RIPLAGGLAT
ERLILHIGQR VRWARGMLQI FRIDNPLFGR GLSWGQRLCY LSAMTSFLFA VPRVIFLSSP
LAFLFFGQNI IAASPLALLA YAIPHMFHAV GTASKINKGW RYSFWSEVYE TTMALFLVRV
TIVTLLSPSR GKFNVTDKGG LLEKGYFDLG AVYPNIILGL IMFGGLARGV YELSFGHLDQ
IAERAYLLNS AWAMLSLIII LAAIAVGRET QQKRNSHRIP ATIPVEVANA DGSIIVTGVT
EDLSMGGAAV KMSWPAKLSG PTPVYIRTVL DGEELILPAR IIRAGNGRGI FIWTIDNLQQ
EFSVIRLVFG RADAWVDWGN YKADRPLLSL MDMVLSVKGL FRSSGDIVHR SSPTKPLAGN
ALSDDTNNPS RKERVLKGTV KMVSLLALLT FASSAQAASA PRAVAAKAPA HQPEASDLPP
LPALLPATSG AAQAGAGDAG ANGPGSPTGQ PLAADSADAL VENAENTSDT ATVHNYTLKD
LGAAGSITMR GLAPLQGIEF GIPSDQLVTS ARLVLSGSMS PNLRPETNSV TMTLNEQYIG
TLRPDPAHPT FGPMSFEINP IFFVSGNRLN FNFASGSKGC SDITNDTLWA TISQNSQLQI
TTIALPPRRL LSRLPQPFYD KNVRQHVTVP MVLAQTYDPQ ILKSAGILAS WFGKQTDFLG
VTFPVSSTIP QSGNAILIGV ADELPTSLGR PQVNGPAVLE LPNPSDANAT ILVVTGRDRD
EVITASKGIA FASAPLPTDS HMDVAPVDIA PRKPNDAPSF IAMDHPVRFG DLVTASKLQG
TGFTSGVLSV PFRIPPDLYT WRNRPYKMQV RFRSPAGEAK DVEKSRLDVG INEVYLHSYP
LRETHGLVGA VLQGVGLARP ASGMQVHDLD VPPWTVFGQD QLNFYFDAMP LARGICQSGA
ANNAFHLGLD PDSTIDFSRA HHIAQMPNLA YMATVGFPFT TYADLSQTAV VLPEHPNAAT
VGAYLDLMGF MGAATWYPVA GVDIVSADHV SDVADRNLLV ISTLATSGEI APLLSRSSYE
VADGHLRTVS HASALDNAIK AVDDPLTAFR DRDSKPQDVD TPLTGGVGAM IEAESPLTAG
RTVLALLSSD GAGLNNLLQM LGERKKQANI QGDLVVAHGE DLSSYRTSPV YTIGTLPLWL
WPDWYMHNRP VRVLLVGLLG CILIVSVLAR ALARHATRRF KQLEDERRKS
