ID J5JGK7_BEAB2 Unreviewed; 648 AA.
AC J5JGK7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=BBA_08396 {ECO:0000313|EMBL:EJP62681.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP62681.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP62681.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP62681.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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; JH725183; EJP62681.1; -; Genomic_DNA.
DR RefSeq; XP_008601715.1; XM_008603493.1.
DR AlphaFoldDB; J5JGK7; -.
DR STRING; 655819.J5JGK7; -.
DR GeneID; 19891408; -.
DR HOGENOM; CLU_013022_2_1_1; -.
DR InParanoid; J5JGK7; -.
DR OrthoDB; 2103951at2759; -.
DR Proteomes; UP000002762; 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:SF45; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJP62681.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 103..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 526..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 595..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 648 AA; 74008 MW; 29CCF38CEEDF618B CRC64;
MRDSKEAQPS LEEIRIIQEL CPPQQAVLAA EPGSRASSIN RQINGILPHG IQTPQTDASW
NSHGADSDIS FSSAVQQEEA KLRWDADAEL KRLSKTLLRM QKWGLISGLV IINGTLIYSA
LKFWQVYYLF IVLLSSNTVL QVLMIVCIIG TWTWKHILCG WRKPKKETTV PDEPEKLVLL
LPCYNETPEE LSRSLDSLVE QENLDSHPRL ILIVVDGNVR GPGMTKTTQR YLLEDILEPG
PRRVFANGYR ARDGLLMPVR VQTGTYRGIP YILVGKKYNQ GKRDSLCFAR SLLYHYHYHD
RLRTTADNAV TTMFHNDLFA HLGTALLQRG LCTIDYLVGM DADTVFDRRC VWEMLRAMRA
ADPSVVVGVC GHVCVDFGAR RFRLWSLYQS VEYAQTQGLR RMFQSRVTGK VSCLPGCCQL
LRVDEATFGD VVLRRRFGYC PKPNDVMTRH IMGSYSEDSI HASIIFSLFP DRQTAQALRA
KAYTTVPQGW RVFLSQRKRW ALGSISNEFV MIFRPCILWV ERLQSVVAVL TWAITPFIVA
ALAEMIMLLV KHGREVIQDP VFISLLSLLW VRYLYSFCIG FWLPQSNLER IQYFVGFFLH
FFTSPFMNII ILVYSLMHSD DFQWGKTREV IQEDGESNAD GQGGRGNH
//
