ACSA1_NOVHA
ID ACSA1_NOVHA Reviewed; 1550 AA.
AC Q76KJ8; P21877; P37717;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 Novacetimonas hansenii (Komagataeibacter hansenii).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Novacetimonas.
OX NCBI_TaxID=436;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23769 / NCIMB 8246;
RA Kawano S., Tajima K., Uemori Y., Yamashita H., Erata T., Munekata M.,
RA Takai M.;
RT "Cloning of cellulose synthesis related genes from Acetobacter xylinum ATCC
RT 23769 and ATCC 53582: comparison of cellulose synthetic ability between
RT ATCC 23769 and ATCC 53582.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC STRAIN=ATCC 23769 / NCIMB 8246;
RX PubMed=8300521; DOI=10.1128/jb.176.3.665-672.1994;
RA Standal R., Iversen T.-G., Coucheron D.H., Fjaervik E., Blatny J.M.,
RA Valla S.;
RT "A new gene required for cellulose production and a gene encoding
RT cellulolytic activity in Acetobacter xylinum are colocalized with the bcs
RT operon.";
RL J. Bacteriol. 176:665-672(1994).
RN [3]
RP 3D-STRUCTURE MODELING, AND MUTAGENESIS OF ASP-188; ASP-189; ASP-236;
RP ASP-333; GLN-369; ARG-370 AND ARG-372.
RC STRAIN=ATCC 23769 / NCIMB 8246;
RX PubMed=11430986; DOI=10.1016/s0031-9422(01)00048-6;
RA Saxena I.M., Brown R.M. Jr., Dandekar T.;
RT "Structure-function characterization of cellulose synthase: relationship to
RT other glycosyltransferases.";
RL Phytochemistry 57:1135-1148(2001).
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 -!- 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 -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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}.
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DR EMBL; AB091060; BAC82543.1; -; Genomic_DNA.
DR EMBL; M96060; AAA16971.1; -; Unassigned_DNA.
DR PIR; S13732; C36963.
DR AlphaFoldDB; Q76KJ8; -.
DR SMR; Q76KJ8; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
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 c-di-GMP; Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1550
FT /note="Cellulose synthase 1"
FT /id="PRO_0000409025"
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 708..731
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 COMPBIAS 708..726
FT /note="Polar residues"
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 MUTAGEN 188
FT /note="D->N: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11430986"
FT MUTAGEN 188
FT /note="D->P: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11430986"
FT MUTAGEN 189
FT /note="D->Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11430986"
FT MUTAGEN 236
FT /note="D->Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11430986"
FT MUTAGEN 333
FT /note="D->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11430986"
FT MUTAGEN 369
FT /note="Q->M: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11430986"
FT MUTAGEN 370
FT /note="R->P: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11430986"
FT MUTAGEN 370
FT /note="R->Q: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11430986"
FT MUTAGEN 372
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11430986"
SQ SEQUENCE 1550 AA; 168183 MW; E62AEDA3F83D8C6B CRC64;
MPEVRSSTQS ESGMSQWMGK ILSIRGAGLI 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 SSPTKPSAGN
ALSDDTNNPS RKERVLKGTV KMVSLLALLT FASSAQAASA PRAVAAKAPA HQPEASDLPP
LPALLPATSG AAQAGSGDAG ADGPGSPTGQ PLAADSADAL VENAENTSDT ATVHNYTLKD
LGAAGSITMR GLAPLQGIEF GIPSDQLVTS ARLVLSGSMS PNLRPETNSV TMTLNEQYIG
TLRPDPAHPT FGPMSFEINP IFFVSGNRLN FNFASGSKGC SDITNDTLWA TISQNSQLQI
TTIALPPRRL LSRLPQPFYD KNVRQHVTVP MVLAQTYDPQ ILKSAGILAS WFGKQTDFLG
VTFPVSSTIP QSGNAILIGV ADELPTSFGR PQVNGPAVLE LPNPSDANAT ILVVTGRDRD
EVITASKGIA FASAPLPTDS HMDVAPVDIA PRKPNDAPSF IAMDHPVRFG DLVTASKLQG
TGFTSGVLSV PFRIPPDLYT WRNRPYKMQV RFRSPAGEAK DVEKSRLDVG INEVYLHSYP
LRETHGLIGA 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 ALARHAARRF KQLEDERRKS
