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
//