ID A0A148N5S1_9GAMM Unreviewed; 719 AA.
AC A0A148N5S1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=AXA67_12780 {ECO:0000313|EMBL:KXJ39916.1};
OS Methylothermaceae bacteria B42.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylothermaceae.
OX NCBI_TaxID=1798802 {ECO:0000313|EMBL:KXJ39916.1, ECO:0000313|Proteomes:UP000074680};
RN [1] {ECO:0000313|EMBL:KXJ39916.1, ECO:0000313|Proteomes:UP000074680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B42 {ECO:0000313|EMBL:KXJ39916.1};
RX PubMed=26779119; DOI=10.3389/fmicb.2015.01425;
RA Skennerton C.T., Ward L.M., Michel A., Metcalfe K., Valiente C., Mullin S.,
RA Chan K.Y., Gradinaru V., Orphan V.J.;
RT "Genomic Reconstruction of an Uncultured Hydrothermal Vent
RT Gammaproteobacterial Methanotroph (Family Methylothermaceae) Indicates
RT Multiple Adaptations to Oxygen Limitation.";
RL Front. Microbiol. 6:1425-1425(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXJ39916.1}.
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DR EMBL; LSNW01000032; KXJ39916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A148N5S1; -.
DR STRING; 1798802.AXA67_12780; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000074680; 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; PF13632; Glyco_trans_2_3; 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|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 31..47
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 54..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 84..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 402..423
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 435..454
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 511..527
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 539..561
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT DOMAIN 229..440
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT DOMAIN 581..664
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 719 AA; 82092 MW; E5AD54430DC8D645 CRC64;
MKKLAIGLWF LSCLVLAFVA AIQVDNHIQL LLATFLVVLL LLLRLAPRLG YLRVLFLSIC
AFLVLRYGVW RVTSTLNYDD FPSFSAAILL FAAEVYGMGL FFLSSFVNAR PISRDPPPLP
SDQNQWPSVA VLIPTLNEPQ ELLKVTLTAA LAMDYPKHKF QVYLLDDGAT REKRNSSDPT
TANQAWQRYD ELFQLCHDLG VKYHTRQENA QAKAGNLNAI LPEIRQDLIL VLDSDHVPTV
DFLQKTVGFF IENSKLFLLQ TPHFFINPDP LEKNLEFSYQ IPSENHMFYE AIQAGLDFWE
ASFFCGSAAL LRMDALRDCG GFSGKTVTED AETALLLHSQ GWQSKYILTP LISGLQPETF
TSFVAQRVRW AQGMLQLLLS RNPLTLKGLK PWQRLGYASN MVFWLFPFAR VVFLISPLFF
LYFGLKIYDA NGEEILSYAV PYLMALILLN HYLFGRVRWF MVSDIYESMQ SLFLLPAIIN
VLKNPISPSF KVTPKIENVQ NDTISPLAKP FYLLILVNTL AIFLGIYKFN TLPEQRTLVL
ITLAWAIFNG IIIMTSLGAL YERRQRRISP RLPAGDISAM LILQNRDEIP VKIRDLSVGG
ISILIAESIL RELSGDIHLK LHHPIDNETF IIRVAVANQG EMDGFTRIGL RFVTDNQEEY
RNLVLLVHGS SERWQQLLKN RDRDFGILAS FRILIKNGFY HAWFHLKTLL FYRNSTEFG
//
