ID A0A1V6QUJ2_9EURO Unreviewed; 755 AA.
AC A0A1V6QUJ2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=PENSOL_c037G04217 {ECO:0000313|EMBL:OQD92893.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD92893.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD92893.1}.
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DR EMBL; MDYO01000037; OQD92893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QUJ2; -.
DR STRING; 60172.A0A1V6QUJ2; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000191612; 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 CDD; cd00761; Glyco_tranf_GTA_type; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000191612};
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 16..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 504..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 538..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 85647 MW; A9E6886FE22FEE7F CRC64;
MIISQRDLLT WPTKDIIYLS IVGPLMLAAL FEWILWLGAF IYCLIKVWMK ADHWSIRVLA
VVMIFLFTVL RLAFLPVMLV TLPLPPQITV DLPHEMVHGF QVFAFWAFSI LLIGPWLFCI
YGLTTNSLGR KKRIKRVLDD RTAPKTVVVM PVYKEDPGVL IKAINSVVDC DYPANCIHVF
LSYDGGKVDE PYLRVLDHLG IPITLESYPQ SIDCIYKGAR ITVSRFKHGG KRNCQKHTFK
LIDKVYAEYL KRHDNLFVLF IDSDCILDRV CLQNFMYDME LKPGSKRNML AMTGIITSTT
ERNSLLTILQ DMEYVHGQLF ERSVESGCGA VTCLPGALTI LRFSAFRKMA KYYFSDKAEQ
CEDLFDYGKC HLGEDRWLTH LFMIGATERY QIQLCMSAFC KTEAVQTFST LLKQRRRWFL
GFITNEVCMI TDVRLWVRYP LLCLVRFMQN TIRTTALLFF IMIIALITTS KKVDDLPVGF
MGVSLGLNYL LMLYFGLRLG RYKAWLYPIM FIVNPFFNWI YMVYGIFTAG QRTWGGPRAD
AATADDHTTP GEAVERAKEQ GDELNVNVDT FRNSLVRRRS VPVRPSENVE GRFAPAKQLL
DGFYVNTAGP GPALARMVNA MENPRTSQYQ SPPLFRQPND SVLTISSDCG SSSVITPQNV
ETLLMSEEDQ KKLYYARQGR AAAGSVTFDG HNSENSFDDG VALRPMGSAS EHDDLGLTPP
LGAYHTGRSE STPPVYTEPE HVVPSDLAPS SFQTP
//
