ID A0A0P7XMQ7_9RHOB Unreviewed; 795 AA.
AC A0A0P7XMQ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming] {ECO:0000256|RuleBase:RU365020};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU365020};
GN Name=bcsA {ECO:0000313|EMBL:KPQ18017.1};
GN ORFNames=HLUCCO18_03095 {ECO:0000313|EMBL:KPQ18017.1};
OS Rhodobacteraceae bacterium HLUCCO18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ18017.1, ECO:0000313|Proteomes:UP000050333};
RN [1] {ECO:0000313|EMBL:KPQ18017.1, ECO:0000313|Proteomes:UP000050333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ18017.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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:KPQ18017.1}.
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DR EMBL; LJSY01000004; KPQ18017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7XMQ7; -.
DR STRING; 1666917.HLUCCO18_03095; -.
DR PATRIC; fig|1666917.4.peg.512; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000050333; 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; 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; PF13641; Glyco_tranf_2_3; 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|RuleBase:RU365020};
KW Glycosyltransferase {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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 39..55
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 101..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 447..466
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 519..543
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
SQ SEQUENCE 795 AA; 88658 MW; 99D060F7DDE98901 CRC64;
MSRNRFQRRA VVPVFLALVW VALVVPIVVV ASLPTSTEVQ ALLGVIAVVL VAILKPFTRT
SIVARLSLLA VASVLVLRYW IWRLLESLPS PEQPVSLAAA LLLFAIETYA IAVFMLTAFI
NADPKDRPLP RRVKAEELPT VDILVPSYNE PTDMLSVTLS AAKHIHYPRE KLRVVLCDDG
GTDQRCNHPD PQIAETSKTR RAELQKLCRE LGVLYSTRAR NEHAKAGNMS AALSRLDGDL
VVVFDADHVP SRDFLARTVG YFVENPRLFL VQTPHFFLNS DPVERNLGLA PSCPAENEMF
YSDIHRGLDR WQGAFFCGSA AILRRTALNE AGGFSGETIT EDAETALDIH AKGWESLYVN
RAMIAGLQAE TFASFIQQRG RWATGMVQML LLKNPLFRPG LKPAQRLCYI NSMSFWLFPL
VRLSFLIIPL FYLFFGLEIF VASGDEVLAY AISYLVVSFM VQNALFAHVR WPLISEVYEV
AQAPYLAIQI FKTILRPRAA KFAVTAKDET LAEDFISPIY LPLLLLFLLM VVGVAAAGIR
WVAFPGDRGV IAIVGAWAVF NMLLAALALR SVAEKQQRRA VPRVQMEVDA AAWRPNAGGK
GPELRATIVD ASTSGLRLEI PPPPHGSPAA ERISDIAQGD EIVLRPRFPD APDLERDIRA
TVQIVQTGAE GIAIGVRFVP DQPMTAREAV AYLIFNDSDH WRRRREEQFK ARGLIHGLLY
VLWLAVTSIP RTFSDFAKEP ARRRRKEEFA EESEVPVHLL AFGADFDPGP PKRSAERRDN
EDDVLDFILD EVKRA
//
