ID M7V429_BOTF1 Unreviewed; 775 AA.
AC M7V429;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=BcDW1_325 {ECO:0000313|EMBL:EMR91012.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR91012.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer.
CC {ECO:0000256|ARBA:ARBA00024009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00000319};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KB707680; EMR91012.1; -; Genomic_DNA.
DR AlphaFoldDB; M7V429; -.
DR STRING; 1290391.M7V429; -.
DR HOGENOM; CLU_012773_0_0_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF41; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 713..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 88424 MW; E80D11699BA7609C CRC64;
MVQYDTSPWP VRDIVYTAIM GSVMLAAFLE WFLWLAAFMY CLFKVFQKAE HWSVRVLSII
VAIIFFLLRA IYLPIMVVTL PLPEGVTQYF PKEMVSFLQW FGFWSFAALL TIPWLFCVYQ
IVTNSLGRKK RIKQVLDEHS APKVVIVMPC YKEEPDILVT AIDSIVDCDY PPSCIHVFLS
FDGDQEDELY LKTIEALGVP LSLDSYPKSI DVTYRTARIT VSRFPHGGKR HCQKATFKLI
DKVYTEYLKR NDNLFILFID SDCILDRVCL QNFMYDMELS PGNTRDMLAM TGVITSTTKK
HSLITLLQDM EYIHGQLFER TVESGCGSVT CLPGALTMLR FSAFRRMAKY YFADKAEQCD
DLFDYGKCHL GEDRWLTHLF MIGAKKRFQI QMCTSAFCKT EAVQTYQSLI KQRRRWFLGF
ITNEVCMLTD IRIWKRYPIL AVVRFMQNTI RTTALLFFIM VLSIVTTTKK VQDLPVGFIG
ISLGLNWLMM IYFGAKLRRF KIWLYPLMFI INPFFNWYYM VYGIFTCGQR TWGGPRADAG
AADSTTSPQQ VIEAAEEAGD ELNVIPETFK PAAEARNNQV VRRPTLPLLP PTRLEGRFAA
AERLPGGWYE HVNDSLTSVA VGRVAPSGRN PTGSRESIDS YVSGFTGTNS VYMPRRVESI
MGEEDRKKYE IAQANQKAPA GAYYNQGYVY EIPDGPEAKG SFQDSVESLA SMDGTTSNSL
AVPQASSYRN GRSPLGRLSL IRSNSRDDPI EMDDQRSDRD HHSDSSNSPE PKPKR
//
