GenomeNet

Database: UniProt
Entry: A0A157SA43_9BORD
LinkDB: A0A157SA43_9BORD
Original site: A0A157SA43_9BORD 
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}.
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; 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
//
DBGET integrated database retrieval system