ID   A0A1Z1WBH5_9ACTN        Unreviewed;       681 AA.
AC   A0A1Z1WBH5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE            EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN   ORFNames=SMD44_03150 {ECO:0000313|EMBL:ARX83722.1};
OS   Streptomyces alboflavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX83722.1, ECO:0000313|Proteomes:UP000195880};
RN   [1] {ECO:0000313|EMBL:ARX83722.1, ECO:0000313|Proteomes:UP000195880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDJK44 {ECO:0000313|EMBL:ARX83722.1,
RC   ECO:0000313|Proteomes:UP000195880};
RA   Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT   "Streptomyces alboflavus Genome sequencing and assembly.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP021748; ARX83722.1; -; Genomic_DNA.
DR   RefSeq; WP_030358272.1; NZ_RHGC01000004.1.
DR   AlphaFoldDB; A0A1Z1WBH5; -.
DR   STRING; 67267.GCA_000716675_01366; -.
DR   KEGG; salf:SMD44_03150; -.
DR   eggNOG; COG1215; Bacteria.
DR   OrthoDB; 9806824at2; -.
DR   Proteomes; UP000195880; 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:UP000195880};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ARX83722.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        425..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        458..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        542..560
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        566..585
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          256..452
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF13632"
FT   REGION          594..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..657
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  75835 MW;  B046F3AE075A49BA CRC64;
     MTSTPTGQGS NDPSQTTQLR VLSNRTGGFR RIKKSLPRYD YEHYSRLAGP LTQPDPAKPY
     KVQYRSLLSQ EPHRLRAALM LGAAPLLSLV LLAWLLQPEH WTERDYVAND WLPVLDIVML
     VSIGLIEFFR CMNVLSNAHA TLVARDPIPV VPENGTRVAF LTSFVPGKEP IEMVTKTLEA
     AVKLRHRGLL HIWLLDEGDD PEVKEVCARL GVHHFSRKGI AKWNQAKGPH RAKTKHGNYN
     AWLDAHGDGY DYFASVDTDH VPMPNYLERM LGFFRDPDVG FVIGPQVYGN YDTFVTKAAE
     SQQFLFHALI QRAGNAYGSP MFVGTSNAVR ISALKQIGGL YDSITEDMAT GFEIHRHKNP
     ATGRKWKSVY TPDVLAVGEG PNAWTDFFTQ QLRWSRGTYE TILKQFWKAP FTLPPGRFFN
     YTMMVIFYPM SAMNWILAAL SCALFLGLGA SGVNIDPTIW LMLYGNASAL QIGLYIWNRR
     HNVSPHEPEG SGGVAGMVMS ALSAPIYARS LMDAALRRKS KFVVTPKGDS ASPDTLFGTF
     RIHLFFILVF AGSIAAAYVY DHAHPAMIIW ATFALLITAA PIFAWRHGMR QEKKKAAAPA
     AGPTEPRVPQ PRHAAPTVHA PQPIPQQQYG QQHPPQPYAP QQYAPHSAPP HARPAPHAPQ
     QKPSWASNDE TMQTALGSHE Q
//