ID D5RT22_9PROT Unreviewed; 627 AA.
AC D5RT22;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming] {ECO:0000256|RuleBase:RU365020};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU365020};
DE Flags: Fragment;
GN Name=celA {ECO:0000313|EMBL:EFH09547.1};
GN ORFNames=HMPREF0731_4234 {ECO:0000313|EMBL:EFH09547.1};
OS Pseudoroseomonas cervicalis ATCC 49957.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=525371 {ECO:0000313|EMBL:EFH09547.1, ECO:0000313|Proteomes:UP000005324};
RN [1] {ECO:0000313|EMBL:EFH09547.1, ECO:0000313|Proteomes:UP000005324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49957 {ECO:0000313|EMBL:EFH09547.1,
RC ECO:0000313|Proteomes:UP000005324};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes
CC uridine 5'-diphosphate glucose to cellulose.
CC {ECO:0000256|RuleBase:RU365020}.
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 Evidence={ECO:0000256|RuleBase:RU365020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU365020};
CC -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC {ECO:0000256|RuleBase:RU365020}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU365020}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFH09547.1}.
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DR EMBL; ADVL01000772; EFH09547.1; -; Genomic_DNA.
DR AlphaFoldDB; D5RT22; -.
DR HOGENOM; CLU_011907_3_0_5; -.
DR OrthoDB; 9806824at2; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000005324; Unassembled WGS sequence.
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 CDD; cd06421; CESA_CelA_like; 1.
DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR InterPro; IPR003919; Cell_synth_A.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR03030; CelA; 1.
DR PANTHER; PTHR43867; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR PANTHER; PTHR43867:SF2; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR PRINTS; PR01439; CELLSNTHASEA.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW c-di-GMP {ECO:0000256|RuleBase:RU365020};
KW Cell inner membrane {ECO:0000256|RuleBase:RU365020};
KW Cell membrane {ECO:0000256|RuleBase:RU365020};
KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916,
KW ECO:0000256|RuleBase:RU365020};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU365020};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365020};
KW Reference proteome {ECO:0000313|Proteomes:UP000005324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365020};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365020};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365020}.
FT TRANSMEM 38..54
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 90..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 401..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 450..473
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 494..518
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 538..555
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT DOMAIN 140..309
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT REGION 608..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 627
FT /evidence="ECO:0000313|EMBL:EFH09547.1"
SQ SEQUENCE 627 AA; 68945 MW; F9F770B19727924B CRC64;
MPPMRRLLPA GPLLWGLLTL AGATLGLTFV VAPLEAEQQA WLALAGFLVF LLVGRAPGRP
ALFFLVALST LISLRYLYWR VTETLDYSGF FATFLGTGLV LAELYAVIAL LLSYFQQLWP
LERKPVPLPA DPAEWPVVDV FIPTYNEPLE VVKPAVFAAL SMDWPRDKLR VHILDDGRRE
DFRQFAGEAG CGYLIRPDNK GAKAGNINHA MTKTDGEYIV IFDCDHVATR AFLQLTIGWM
IRDRGIGMLQ TPHHFYSPDP FERNLASGKR VPNEGLLFYG LVQQGNDLWN ATFFCGSCAV
LRRSALEQVG GVPTETVTED CHCSLKMQRL GWRTAYLRVP LAAGLATDRL ITHIGQRMRW
ARGMIQIFRV ENPLLGPGLK LYQRLCYLNA QWHFLFPLPR VVFLTAPLAF LLLGQSIIAA
SPLAIVAYAG PHIVHSIGTN SRLQGRVRHS FWSEIYETVL ALYLLPVVLA TLFDPKKGKF
NVTDKGGTLQ EGYFDLRAVA ANFVLAIFLV LGLLSGIYGM AANAPASQEF QANLLNSVWV
ALSLVTVMAG LAVGRERRQV RERHRVSARL PSIAILPDGR RVEGESVDLS LGGALLIMPR
PEGFGAPAVP APAASAPAAT DQAAAAQ
//
