ID A0A160P5L9_STRLU Unreviewed; 648 AA.
AC A0A160P5L9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=SLA_5290 {ECO:0000313|EMBL:BAU86171.1};
OS Streptomyces laurentii.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=39478 {ECO:0000313|EMBL:BAU86171.1, ECO:0000313|Proteomes:UP000217676};
RN [1] {ECO:0000313|EMBL:BAU86171.1, ECO:0000313|Proteomes:UP000217676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31255 {ECO:0000313|EMBL:BAU86171.1,
RC ECO:0000313|Proteomes:UP000217676};
RA Doi K., Fujino Y., Nagayoshi Y., Ohshima T., Ogata S.;
RT "Complete Genome Sequence of Thiostrepton-Producing Streptomyces laurentii
RT ATCC 31255.";
RL Genome Announc. 4:e00360-16(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AP017424; BAU86171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160P5L9; -.
DR KEGG; slau:SLA_5290; -.
DR Proteomes; UP000217676; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06421; CESA_CelA_like; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
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 SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000217676};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAU86171.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 232..424
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT REGION 622..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 71217 MW; FCCAEECA1FAEA4FC CRC64;
MWEAPVRPGG YDYDTYSRLA GPLTEPEPEP GSPFGGYQVR YRSLLSKEPH RIRAVLLMGL
APLLSALLLV YLVWPSHWTV REGDEAWRIP YDTVMLVSIG LICFFMLVNV TSIAHATLVA
RDPIPVHPEP GTRVAFLTTY VPGKEPLTMV RATLEAAVRL RHDGRLDVWL LDEGDDPDAR
ALCEELGVRH FTRAGVPEWN RPKGVHKART KHGNYNAWLA GHGAGYDFFA SVDTDHVPLP
DFLERMLGYF RDPDVAFVVG PQVYGNYAAG VTKAAESQQF LFHALVQRAG NRYRSPMFVG
TNNVVRVKAL LQIGGLVDSV TEDMATGFEL HRRRNPRTGH PWRSVYTPDV LAVGEGPASW
TDFFNQQLRW SRGTYETILK QYWKAPFRTP PGRLLNYTLM LVYYPMTAVN WLLGILSCVL
FLWLGASGTQ VSSSVWLMIY SDAVALQVGA YLWNRRHNVS PHEPEGSGGL AGMVLSALCA
PIYLMSLGSA VLRTRGRFVV TPKGGEASPD RLATFRVHLF WVAVLVASLI ASVRLGHTHA
AMRTWAVVAL VIALAPAGVW TTGRLRAGDG MRAKVRGAAV RIRRTRLAVR LPYEVRLPFG
ARVRIETRGP ADTPEGVTLV TTPAPAAPAA SPTTAAAAAT GSTTTGGN
//
