ID T0HQT6_9SPHN Unreviewed; 1122 AA.
AC T0HQT6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming] {ECO:0000256|RuleBase:RU365020};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU365020};
GN ORFNames=L288_01410 {ECO:0000313|EMBL:EQB14528.1};
OS Sphingobium quisquiliarum P25.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1329909 {ECO:0000313|EMBL:EQB14528.1, ECO:0000313|Proteomes:UP000015525};
RN [1] {ECO:0000313|EMBL:EQB14528.1, ECO:0000313|Proteomes:UP000015525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P25 {ECO:0000313|EMBL:EQB14528.1,
RC ECO:0000313|Proteomes:UP000015525};
RX PubMed=24029763;
RA Kumar Singh A., Sangwan N., Sharma A., Gupta V., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium quisquiliarum Strain P25T, a Novel
RT Hexachlorocyclohexane (HCH)-Degrading Bacterium Isolated from an HCH
RT Dumpsite.";
RL Genome Announc. 1:e00717-13(2013).
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|ARBA:ARBA00000122,
CC 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|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. 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:EQB14528.1}.
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; ATHO01000009; EQB14528.1; -; Genomic_DNA.
DR AlphaFoldDB; T0HQT6; -.
DR PATRIC; fig|1329909.3.peg.258; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000015525; 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; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR InterPro; IPR003919; Cell_synth_A.
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 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; PF03170; BcsB; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF07238; PilZ; 1.
DR PRINTS; PR01439; CELLSNTHASEA.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF141371; PilZ domain-like; 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 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 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 33..49
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 56..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 93..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 403..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 446..468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 498..517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 529..550
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 704..725
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT DOMAIN 135..302
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 555..651
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
FT REGION 730..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 124739 MW; 1D8BA3688A0DE855 CRC64;
MRLLESSPAK WLTALFAALL AALVIGVPMD LEAQWLFTGI TIIGAIVLSR SRTRKTTLAL
GILSVLVSTR YMFWRTTQTL EFGTPLEFLL GTGLYLAEIY AWVILLLGFL QTSWPLNRPV
VEIEGEPDQW PFVDVFIPTY NESLSIVRNT VFAAMDMDYP ADRFRVYILD DGRRPEFRAF
ARQVGCGYLT RPDNLHAKAG NLNAAMKKTD GELIAIFDCD HVPTRAFLQM TVGWFQKDAK
LALMQTPHHF YSPDPAQRNL RTVDDLPGEG DLFYGNVQGG NDLWNAAFFC GSCAIIRREA
LQQTNGFAGE TVTEDAHTAL KLQRMGWSTA YISARLSAGL ATERLVLHIG QRIRWARGMT
QILRIDNPLL GPGLKWQQRL CYLNAMLHFQ FPLPRIVFLT SPLAYLIFGQ NIIHASASLI
FAYAAPHLYC SMVSGARSQG GDRRPFWGEI YETILAFHLV PATVLTLFNP RKGKFNVTDK
GSLLDRTYFD LGTVKPHLIC IGLMLFGITL GVVKRVFFPH LFNIQTDTLL LNTAWASFSL
IILLAAVSVA RETRQAREHI RIETQLPVTI YMQDGHVFDA TTIDLSMGGT AVALPQDVSL
RDRTVTHISL PMGDEKLTIP VDTIRSDHGQ AFLRFKPLDL TLSRHLVRAI LGRADAWQPV
APPRPVSGLR SLWDIIVVDF TTLKRLFRLN RKERRSLKRE RTHAAAAVAG KSAALLLAAI
TLMGLPQETR AQSAPAREAS SAPPAGARQQ RLSFRDLQIK TPIRLQGSRG EIGIPFGMRR
NEVVTRANLT LNLAWSPAML GDLSQLVVLL NGEVVRIIPL RPADAGGQAV TIPVNPALFL
PGDNRLNLRL LGHYTRDCED PFHSSLWANV SNVRSWFDLT VQTLPISPDL ARLPGPFFDR
NDNLPLRLPF VFAGTPGNSE LEAAASIASW FGGMASYRGF SFKPLYNQLP QGNGIVFLLP
NRPVAGLNMQ VRGPAAAVIR NPRDSFGQLL VIMGRNTQEL KLAAAAIASG RGVFGGAQMA
FDNVRIPAYP RYSAPRWIAT DRPVRLGELT SAYALQGLGL PPGPLSARFR ITPDLFFWPR
QGGRLELRYR YPTADWLDKR GSRLDLSINN QYLRTLPLSG GD
//
