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Database: UniProt
Entry: E6WHB6_PANSA
LinkDB: E6WHB6_PANSA
Original site: E6WHB6_PANSA 
ID   E6WHB6_PANSA            Unreviewed;       701 AA.
AC   E6WHB6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
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};
DE   Flags: Precursor;
GN   OrderedLocusNames=Pat9b_0114 {ECO:0000313|EMBL:ADU67441.1};
OS   Pantoea sp. (strain At-9b).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU67441.1, ECO:0000313|Proteomes:UP000001624};
RN   [1] {ECO:0000313|EMBL:ADU67441.1, ECO:0000313|Proteomes:UP000001624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-9b {ECO:0000313|EMBL:ADU67441.1,
RC   ECO:0000313|Proteomes:UP000001624};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT   "Complete sequence chromosome of Pantoea sp. At-9b.";
RL   Submitted (DEC-2010) 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}.
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DR   EMBL; CP002433; ADU67441.1; -; Genomic_DNA.
DR   RefSeq; WP_013507310.1; NC_014837.1.
DR   AlphaFoldDB; E6WHB6; -.
DR   STRING; 592316.Pat9b_0114; -.
DR   KEGG; pao:Pat9b_0114; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_011907_5_0_6; -.
DR   OrthoDB; 9806824at2; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000001624; Chromosome.
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; IPR005150; Cellulose_synth.
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; PF03552; Cellulose_synt; 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|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        28..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        53..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        82..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        378..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        408..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        494..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        524..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   DOMAIN          131..301
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   DOMAIN          550..644
FT                   /note="PilZ"
FT                   /evidence="ECO:0000259|Pfam:PF07238"
SQ   SEQUENCE   701 AA;  79002 MW;  05BD46A41D1E80A2 CRC64;
     MSKLAFYLLL LVLAPVAAVI IITPMDSQKQ YIFGLISIGM LFLMGLSKSR KITVVMVILS
     ALMSTRYIWW RTTETLQFNS EIEAILGIGL YLAELYVWLI LILGFLQTTW PLKRTIEPLP
     DDTSLWPTVD VYVPSYNESL DVVRDTVLAA QCIDYPRDKL KIYLLDDGKR SEFAMFAADV
     GVGYITRDDN RHAKAGNLNH AMKITKGELI CVFDCDHVAT RTFLQATVGP FLKDPKLALL
     QTPHYFYSPD PFERNLRAAR SIPNEGSLFY GPVQQGNDNW NATFFCGSCA VIRRSALEEI
     GGFAVETVTE DAHTALKMQR LGWGSAFLSI PLAAGLATER LGLHVIQRTR WARGMTQIFR
     VDNPLFGRGL KWQQRLCYLN AMLHFQFGLP RVAFLTAPLA YLLFNLNIIH SSASLIFAYV
     LPHLVMSLYV NSRMNGRFRY TFWGEIYETV MCFHLVIPTI LTMFSPKHGK FNVTDKGGVL
     DQGFFDFHIV RPHVIVAALL TIGIVAGVVR ATMHDYFGVD PYVIALNVGW AVFSLIILMA
     AIAVARETKQ VRKTIRIEVQ IPAIIHYASG ISSRTMTSDL SMGGAQLDAP DGRHEYDEIE
     EIDLLLKSGA ITIPVSKISG DDETIRLRFE AMPLSRRREL VRVVLARADA WIQPQYKQDN
     PLLSLGTIVR TVFELFWLTW KDRRNKGKQD AQPAVKEDSA A
//
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