ID A0A1G6D5I2_9STRE Unreviewed; 741 AA.
AC A0A1G6D5I2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=Cellulose synthase (UDP-forming) {ECO:0000313|EMBL:SDB40319.1};
GN ORFNames=SAMN02910293_01984 {ECO:0000313|EMBL:SDB40319.1};
OS Streptococcus henryi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=439219 {ECO:0000313|EMBL:SDB40319.1, ECO:0000313|Proteomes:UP000182508};
RN [1] {ECO:0000313|EMBL:SDB40319.1, ECO:0000313|Proteomes:UP000182508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-4 {ECO:0000313|EMBL:SDB40319.1,
RC ECO:0000313|Proteomes:UP000182508};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FMXP01000032; SDB40319.1; -; Genomic_DNA.
DR RefSeq; WP_074486526.1; NZ_FMXP01000032.1.
DR AlphaFoldDB; A0A1G6D5I2; -.
DR STRING; 439219.SAMN02910293_01984; -.
DR Proteomes; UP000182508; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd06421; CESA_CelA_like; 1.
DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009875; PilZ_domain.
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; PF13641; Glyco_tranf_2_3; 1.
DR Pfam; PF07238; PilZ; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF141371; PilZ domain-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000182508};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 478..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 508..605
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
SQ SEQUENCE 741 AA; 86662 MW; FB72B625EDF11A3A CRC64;
MTIRQRLLYA LAFLTTVFYL SWRIISTIPW RGSLFAIIFA LLLWFSEVTS SITAYIIIWN
KQKNLKLEKP IIRDNQYPDI DVFIATHNED TDLLYKTINA CTYMAYPDKS KVHIYICDDT
NRSEVAKLAQ DFGVGYFGLS DNKHAKSGNL NNGLNQTSSP LVATFDADMI PYRDFLLETV
PYFIEQLEAD EKDEELDTRI GLIQTPQSFY NTDIFQFNLF SEDTLPNEQD FFSKGVNVLN
NARGAAVYTG SNTVLYRKAI EDAGGFPINT ITEDFELGVR MNTKGYVNYS TTEPMASGLT
PTDLRSVLKQ RIRWGRGVLN SSYNMNIFFN PKLTLVQRII YINGYLYWWS FFRRLLYILA
PILFTVFHVR VVVANVWLLL FFWLPSYVLT RLSMSDVTNQ YRTQAWGEIV ETILAPYLVA
PLFLEAFGIR EKKFKVTKKS GDSSRWEWLY ALPYLVLWGL SVYGLLTFNY GKFGSELFYG
SVISFWLIHH IINLTFAIFC SLGRPLYRAS ERFAVDDYIM MESWSEKFEV HLSDISETGV
SFFTEEPIYL PRESWLTLYL KSRDYQAKVK AEVVRVYPGN NGWNYGLRFV EIPDQEKREF
LQYIYDRVNH NLPQIHDNWM SILDDLFENI SRRLNKPDLK ETVYNKDALP VIMVNEVIDV
EGRERNLVQT NYAYMTLSDR PTEEEKLGRS TFIDHKGLKF QLEFLDFDFE KEESIYRVKN
LAELQAYPEF NQLAQEWRGR V
//
