ID A0A071LXC7_9ENTR Unreviewed; 876 AA.
AC A0A071LXC7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming] {ECO:0000256|ARBA:ARBA00018714, ECO:0000256|RuleBase:RU365020};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539, ECO:0000256|RuleBase:RU365020};
GN Name=bcsA {ECO:0000313|EMBL:KEA53092.1};
GN ORFNames=DT73_09170 {ECO:0000313|EMBL:KEA53092.1};
OS Mangrovibacter sp. MFB070.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Mangrovibacter.
OX NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA53092.1, ECO:0000313|Proteomes:UP000027726};
RN [1] {ECO:0000313|EMBL:KEA53092.1, ECO:0000313|Proteomes:UP000027726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFB070 {ECO:0000313|EMBL:KEA53092.1,
RC ECO:0000313|Proteomes:UP000027726};
RA Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., Lalitha K.V.;
RT "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
RT Bacterium Isolated from an Aquaculture Farm.";
RL Submitted (APR-2014) 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|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|ARBA:ARBA00005186, 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 -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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:KEA53092.1}.
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; JJMI01000020; KEA53092.1; -; Genomic_DNA.
DR RefSeq; WP_036107157.1; NZ_JJMI01000020.1.
DR AlphaFoldDB; A0A071LXC7; -.
DR eggNOG; COG1215; Bacteria.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000027726; 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; 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; 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 3: Inferred from homology;
KW c-di-GMP {ECO:0000256|ARBA:ARBA00022636, 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|RuleBase:RU365020,
KW ECO:0000313|EMBL:KEA53092.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365020};
KW Reference proteome {ECO:0000313|Proteomes:UP000027726};
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 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 147..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 228..252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 522..540
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 546..567
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 665..690
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT DOMAIN 277..446
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 694..790
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 876 AA; 99538 MW; 176E40970D964E60 CRC64;
MSRLLRCVLT TPVAGALSAQ YRHYRAHRTS LFSAVIGCIW LCLAWCFLPL ENANWQRVRS
NFRLWFPQVN PDKPGPLDVI RILIQGCWLV VLVPGHLSGL AVQKYLSRAA AWRKDYHDWL
TALPGRVKAR AESQQQRREL CHVSPRIRRL VLGVVVLFSL TLSILCITQP FTPLAQFVFL
LLLWGIALVV RRIPGRFPSL MLIVLSLTVS CRYIWWRYTS TLNWNDPLSL MFGLILLFAE
TYAWVVLVMG YFQIAWPLNR HPVPLPEDQS QWPVVDIFVP TYNEDLSVVE GTIYAALGID
WPKDKLNIWI LDDGGRESFR AFAQKVGVRY IARTSHEHAK AGNINNALKY AKGDFVAIFD
CDHVPTRSFL QLTVGWFFKD KKLAMMQTPH HFFSPDPFER NLGRFRKTPN EGTLFYGLVQ
DGNDMWDATF FCGSCAVIRR GPLDEIGGIA VETVTEDAHT SLRLHRRGYT SAYMRIPQAA
GLATESLSAH IGQRIRWARG MIQIFRMDNP LFGKGLKLAQ RLCYANAMLH FLSGIPRLIF
LTAPLAFLLF HAYIIFAPAL MIALFVLPHM VHASLTNSRI QGKYRHSFWS EIYETVLAWY
IAPPTVVALI NPHKGKFNVT AKGGLVEEEY VDWVITRPYL WLVMVNLLGV AVGIWRMFYG
PDHEVLTVVV SLAWVFYNLI ILGGAVAVSV ESKQVRRAHR VEIAMPAAVA RDDGHLFACT
VRDYSGGGLG IHLQGTAAFL QDQKVNLLLN RGDQEFFFPA RVVRVNGQEL GIQLSDLSTQ
QHIDFIQCTF ARADTWALWQ DSFPQDKPME SLLDILKLGF RGYRHLAEFT PSGMKVVFRS
VTTLVDWIVS FIPRRPDAVN EDARQDSAGS TMMTMR
//
