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Database: UniProt
Entry: A8G818_SERP5
LinkDB: A8G818_SERP5
Original site: A8G818_SERP5 
ID   A8G818_SERP5            Unreviewed;       867 AA.
AC   A8G818;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   24-JAN-2024, entry version 77.
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   OrderedLocusNames=Spro_0148 {ECO:0000313|EMBL:ABV39258.1};
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV39258.1};
RN   [1] {ECO:0000313|EMBL:ABV39258.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568 {ECO:0000313|EMBL:ABV39258.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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; CP000826; ABV39258.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8G818; -.
DR   STRING; 399741.Spro_0148; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; spe:Spro_0148; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_011907_5_0_6; -.
DR   OMA; QRLCYAN; -.
DR   OrthoDB; 9806824at2; -.
DR   UniPathway; UPA00694; -.
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   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985};
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        31..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..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        195..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        226..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        520..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        544..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        637..657
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   TRANSMEM        663..688
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365020"
FT   DOMAIN          276..445
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   DOMAIN          692..788
FT                   /note="PilZ"
FT                   /evidence="ECO:0000259|Pfam:PF07238"
SQ   SEQUENCE   867 AA;  98130 MW;  D7C4747B9735A4B0 CRC64;
     MSRVMSLLLV PPVQQAVQTR YRAYRRHGSS AFTAFFTTLL VALGWIFLRF ESPGWQRLRA
     GRAYWFPHLS SSRPRPADVL RYLVQGLWLL VFRTDREPMD HQRFAGWQRL QLRYANWLKT
     IPQRLENAGL EQRSVARLSR MNQRVRRVLF IIVGVLAAIL AILCISQPFD LPAQFVFVLL
     LWGIAMVVRR VPGRLPALML IVLSLTVSCR YLWWRYTATL NWDDPLSLTC GLLLLVAETY
     AWVVLVLGYF QTVWPLNRQP VPMPADSSTW PTIDLLVPTY NEDLGVVKPT IYAALGIDWP
     KEKVTIYILD DGNRPEFKAF AEEVGVKYIA RPTHEHAKAG NINNALKQAT GEFVAIFDCD
     HVPTRSFLQL TMGWFFKDKK LAMLQTPHHF FSPDPFERNL GRFRQTPNEG TLFYGLVQDG
     NDMWDATFFC GSCAILRRSA LDEIGGIAVE TVTEDAHTSL RLHRRGHTSA YIRIPQAAGL
     ATESLSAHIG QRIRWARGMV QIFRLDNPLF GKGLKLAQRL CYANAMLHFL SGIPRLIFLT
     APLAFLLLHA YIIFAPALAI ALYVLPHMIH ASLTNSRIQG KYRHSFWSEI YETVLAWYIA
     RPTTVALFNP HKGKFNVTAK GGLVEEEHVD WVITRPYMFL VILNLAGLFF GVWRLGYGPA
     DEVMTVIISL VWVLYNMTIL GGAVAVAVEA KQVRQAHRVE IAMPAAIARA DGHLFPCTLR
     DYSDGGVGIE MRVADALKDG DKASLLLKRG QQEYSFPCVV TRAFGSKVGI RMVGLSTREH
     IDFIQCTFAR ADTWALWQDG FPEDKPIESL RDVLALGFRG YIRMADYAPP MVRRLLVGTT
     TLIGWIVSFI PHGVGRAPAF SQKETVV
//
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