ID A0A1H7BFV9_9ACTN Unreviewed; 731 AA.
AC A0A1H7BFV9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=SAMN05443287_107254 {ECO:0000313|EMBL:SEJ76583.1};
OS Micromonospora phaseoli.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1144548 {ECO:0000313|EMBL:SEJ76583.1, ECO:0000313|Proteomes:UP000198707};
RN [1] {ECO:0000313|Proteomes:UP000198707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7038 {ECO:0000313|Proteomes:UP000198707};
RA Varghese N., Submissions S.;
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; FNYV01000007; SEJ76583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7BFV9; -.
DR STRING; 1144548.SAMN05443287_107254; -.
DR Proteomes; UP000198707; Unassembled WGS sequence.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SEJ76583.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..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 412..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 233..424
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT REGION 574..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 80049 MW; 806417C2F8C8EFC9 CRC64;
MTDPFEIPVY GRSWARLEAF SRIAGPLTEP PAGQPYRVRY RSMHRVTGNR RIVTAVGIAL
ANICFEVFFL IWLFQPGHLA DTNPGPVAEV ARVANIFVIC SIILVESLRL INVLSLSLAS
VIARDPIPVT PPAGLKVAFL TTIVPSKEPI AVVRDTLRAA KRIRHRGVFD VWLLDEGDDP
DVKAMCAELG VRHFTRKGVD GYNQARGPFR ARTKHGNYNA WVDAHGGGYD VFLSVDPDHV
PLANFAERIL GYFRDPDVAY VVGPQCYKNG EAFVTRAAES QQFPFHSVIQ RAANTYGTSM
LVGTNNAIRI RALRDVGGLS DSITEDMATG LAVHTTRNRV TGRRWKSVYT PDVLSAGDGP
SSWSDYFSQQ RRWSRGTFEL LFGRYWLRFP RLSVGGMLHY TLITTFYPSM AIGWLLGIVN
ALLFLALGVT GMTISPQLWF ALYTDATAFS LWLYLYNRQY NVSPYEPPGS RGLKGMLMSI
ISAPIYAGQL VSTWLRRPAR FVVTPKGTHS SSDGLYTFRA HLGWLAVLVA AIVVAFVRDY
ASPAALLWPV VALLICLAPI ALWRRDLRVI ASAPAGAPDR PDPVQEVRSP DRVGDITMEI
PRVLRDAHLA SRSTGAPRKD DGPAAAGGPR PTRIPRQADP PGTERIQRHD MDATVRFRAS
TGTTPRVDGR SGQGAAPDQR PGGAGAAESA PGPTTEDPAS ATIELAAIRP TESEDRAASR
GERPGWFGSN S
//
