ID A0A157SA43_9BORD Unreviewed; 731 AA.
AC A0A157SA43;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:SAI66776.1};
GN ORFNames=SAMEA3906486_01144 {ECO:0000313|EMBL:SAI66776.1};
OS Bordetella ansorpii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI66776.1, ECO:0000313|Proteomes:UP000076848};
RN [1] {ECO:0000313|EMBL:SAI66776.1, ECO:0000313|Proteomes:UP000076848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050680373 {ECO:0000313|EMBL:SAI66776.1,
RC ECO:0000313|Proteomes:UP000076848};
RG Pathogen Informatics;
RL Submitted (APR-2016) 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|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}.
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DR EMBL; FKIF01000002; SAI66776.1; -; Genomic_DNA.
DR RefSeq; WP_066124610.1; NZ_FKIF01000002.1.
DR AlphaFoldDB; A0A157SA43; -.
DR STRING; 288768.SAMEA3906486_01144; -.
DR OrthoDB; 9806824at2; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000076848; 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 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:UP000076848};
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 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 55..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 113..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 404..422
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 428..449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 521..542
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 548..573
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT DOMAIN 159..328
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 577..673
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 731 AA; 80861 MW; 27E507FDF2DA85BB CRC64;
MTNPSPARAG RRDGAPAWDE TLLAMPLWSK AWVRVLAGLA AAVLFVLAVT VEFGLAEQLM
FTGICVVLAL VLNRMGGRLV TLVMVTLSII VSLRYMYWRV TQTLGFVDPI DMAFGYGLLL
AELYALTVML LSYFQSAWPL QRKPMPMQGD SATWPTIDVF IPTYNEPLSV VRQSVLAAMA
LDWPADKLRV YVLDDGRRAE FRDFCAQAGA GYLTRQDNRH AKAGNINAAL AKTDGEFVAI
FDCDHIPTRS FLQICMGWFV KDPKLAMLQT PHVFFSPDPF ERNLETFRNV PNEGELFYGI
IQDGNDLWNA TFFCGSCAVI RRTHLAEVGG VATESVTEDA LTALKMNRVG FNTAYLAIPQ
AAGLATENLS RHIGQRTRWA RGMAQIIRIN NPLLGRGLKL GQRLCYLNAM LHFFFGLPRV
VFLTTPLAFL FFGAHVFHAS ALMVAAYALP HIFLSSISGA RVQGRFRHSF WNEVYEAVLA
WYIMRPALQT LISPNRAIFN VTAKGGVISK SYFDWELARP YVVLLGLNLL GLVIGVVSMM
AASDLDTVLT ILINVVWTFY NIVITSAAVA VAGEVRQLRN THRVTVDLPA AVALPDGRSI
ACRISDFSQG GVGVVLPKGA QVPQGSTVHI SIFRGDFEGV FPATVSFSRD NRLGLSFQNL
NMDQESELAQ VTFARADTWA SMWGQSKPAS PLVAMRHISS IGLRGFTLLL RYMRDRGMAR
LRRTVPASPK N
//