ID   CHS5_EXODE              Reviewed;        1885 AA.
AC   Q8TGV2;
DT   02-OCT-2024, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   27-NOV-2024, entry version 89.
DE   RecName: Full=Chitin synthase 5 {ECO:0000303|PubMed:14871935};
DE            EC=2.4.1.16 {ECO:0000269|PubMed:18992354, ECO:0000269|PubMed:19431044};
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 5 {ECO:0000305};
DE   AltName: Full=Class-V chitin synthase 5 {ECO:0000303|PubMed:14871935};
GN   Name=CHS5 {ECO:0000303|PubMed:14871935};
OS   Exophiala dermatitidis (Black yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=5970;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=8656;
RX   PubMed=14871935; DOI=10.1128/ec.3.1.40-51.2004;
RA   Liu H., Kauffman S., Becker J.M., Szaniszlo P.J.;
RT   "Wangiella (Exophiala) dermatitidis WdChs5p, a class V chitin synthase, is
RT   essential for sustained cell growth at temperature of infection.";
RL   Eukaryot. Cell 3:40-51(2004).
RN   [2]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12213927; DOI=10.1099/00221287-148-9-2811;
RA   Wang Q., Liu H., Szaniszlo P.J.;
RT   "Compensatory expression of five chitin synthase genes, a response to
RT   stress stimuli, in Wangiella (Exophiala) dermatitidis, a melanized fungal
RT   pathogen of humans.";
RL   Microbiology 148:2811-2817(2002).
RN   [3]
RP   INDUCTION.
RX   PubMed=17937668; DOI=10.1111/j.1574-6968.2007.00920.x;
RA   Liu H., Szaniszlo P.J.;
RT   "Transcription and expression analyses of WdCHS5, which encodes a class V
RT   chitin synthase with a myosin motor-like domain in Wangiella (Exophiala)
RT   dermatitidis.";
RL   FEMS Microbiol. Lett. 276:99-105(2007).
RN   [4]
RP   SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND ZYMOGEN.
RX   PubMed=19431044; DOI=10.1080/10826060902953244;
RA   Abramczyk D., Szaniszlo P.J.;
RT   "Immunoaffinity purification of the class V chitin synthase of Wangiella
RT   (Exophiala) dermatitidis.";
RL   Prep. Biochem. Biotechnol. 39:277-288(2009).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=18992354; DOI=10.1016/j.fgb.2008.10.004;
RA   Abramczyk D., Park C., Szaniszlo P.J.;
RT   "Cytolocalization of the class V chitin synthase in the yeast, hyphal and
RT   sclerotic morphotypes of Wangiella (Exophiala) dermatitidis.";
RL   Fungal Genet. Biol. 46:28-41(2009).
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 (PubMed:19431044). CHS5 is
CC       required for the sustained growth at 37 degrees Celsius and is of
CC       critical importance for virulence (PubMed:14871935, PubMed:18992354).
CC       Especially important at infection temperatures for maintaining the cell
CC       wall integrity of developing yeast buds, elongating tips of hyphae, and
CC       random sites of expansion in sclerotic forms (PubMed:18992354).
CC       {ECO:0000269|PubMed:14871935, ECO:0000269|PubMed:18992354,
CC       ECO:0000269|PubMed:19431044}.
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) + UDP +
CC         H(+); 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:0000269|PubMed:18992354, ECO:0000269|PubMed:19431044};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16638;
CC         Evidence={ECO:0000269|PubMed:18992354, ECO:0000269|PubMed:19431044};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18992354,
CC       ECO:0000269|PubMed:19431044}; Multi-pass membrane protein. Membrane
CC       {ECO:0000255}. Note=Localizes to the regions of cell wall growth in an
CC       actin-dependent fashion. {ECO:0000269|PubMed:18992354}.
CC   -!- INDUCTION: The expression level increases quickly and almost doubles
CC       when cells were shifted to 37 degrees Celsius, compared to cells
CC       maintained at 25 degrees Celsius (PubMed:12213927, PubMed:14871935,
CC       PubMed:17937668). Expression is also increased under additional stress
CC       conditions that are known to initiate development of the sclerotic
CC       morphology (acidic conditions or Ca(2+) limitation induced by EGTA) or
CC       of hyphae (induced by nitrogen limitation) (PubMed:14871935). At least
CC       one negative regulator binding sequence exists in the promoter between
CC       -880 and -680 bp and another regulatory binding site is localized
CC       between bp -680 and -450 bp (PubMed:14871935).
CC       {ECO:0000269|PubMed:12213927, ECO:0000269|PubMed:14871935,
CC       ECO:0000269|PubMed:17937668}.
CC   -!- DOMAIN: Contains an N-terminal myosin motor-like domain with a P-loop
CC       (MMD) that is involved in the actin-dependent localization to the
CC       regions of cell wall growth. {ECO:0000269|PubMed:18992354}.
CC   -!- PTM: Maximal activity requires trypsin activation, suggesting a
CC       zymogenic nature. {ECO:0000269|PubMed:19431044}.
CC   -!- DISRUPTION PHENOTYPE: Leads to hyperpigmentation and loss of viability
CC       in stationary phase at 37 degrees Celsius (PubMed:14871935). Reduces
CC       the virulence in a mouse model of acute infection (PubMed:14871935).
CC       Causes cell wall integrity defects and subsequent abnormal yeast
CC       morphology at 37 degrees Celsius (PubMed:14871935). Does dot lead to
CC       compensation by increased expression of another chitin synthase genes
CC       (PubMed:12213927). {ECO:0000269|PubMed:12213927,
CC       ECO:0000269|PubMed:14871935}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class
CC       myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the chitin synthase
CC       family. Class V subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF469116; AAL79830.2; -; Genomic_DNA.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   VEuPathDB; FungiDB:HMPREF1120_08776; -.
DR   BRENDA; 2.4.1.16; 6682.
DR   PHI-base; PHI:390; -.
DR   GO; GO:0030428; C:cell septum; IEA:TreeGrafter.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   FunFam; 1.10.10.60:FF:000337; Chitin synthase 8; 1.
DR   FunFam; 1.10.10.820:FF:000012; Chitin synthase ChsE; 1.
DR   FunFam; 1.20.58.530:FF:000017; Chitin synthase ChsE; 1.
DR   FunFam; 3.10.120.10:FF:000019; Chitin synthase ChsE; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036037; MYSc_Myo17.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   SMART; SM01117; Cyt-b5; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51998; DEK_C; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; ATP-binding; Cell membrane; Glycoprotein;
KW   Glycosyltransferase; Membrane; Motor protein; Myosin; Nucleotide-binding;
KW   Transferase; Transmembrane; Transmembrane helix; Virulence; Zymogen.
FT   CHAIN           1..1885
FT                   /note="Chitin synthase 5"
FT                   /id="PRO_0000460790"
FT   TRANSMEM        894..914
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        929..949
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1205..1225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1599..1619
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1626..1646
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1653..1673
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..789
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          957..1016
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   DOMAIN          1827..1882
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT   REGION          601..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..690
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   REGION          794..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         99..106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        668
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1043
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1068
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1759
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1790
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1885 AA;  208884 MW;  455A842ED0D426F3 CRC64;
     MATRGNVPAH MQASLPALPA HLQSDTHITA HLASRFHVSL PTARLSSQGL ICLNTFTSST
     RGPNGDKEGS AMGEPEDLAR RAWARLGNRA EDQAFGFFGE SGSGKTTVRS HLLSSFLSFS
     STPLSSKLSL AAFVFDTLTT TKTTTTQTAS KAGLFYELQY DASSNNPTLI GGKLLDHRFE
     RSRISHVPTG ERSFHVLYYL LAGTSAAEKS HLGLDGHVNI TTAGTGLSRS ASVSHKRWRY
     LGHPTQMKVG INDAEGFQHF KNALRKLEFP RTEIAEICQV LAAILHIGQL EFGTGQATLT
     AAEESGGYSH EGGETVTVVK NRDTLAIVAA FLGLGVQDLE ESLRYKTRTI HRERVTVMLD
     TKGARENADE LATTLYSLLV TYIIESINQR VCAAEDSVAN TISIVDFPGF ADHSSTGSVL
     DQLLNNAANE SLYNTCLHSI FEKTAEMLES EEVSVPATSY FDNSDAVRGL LKHGNGLLAI
     LDDQTRRGRT DVQFLESLRK RFENKNKAIT VGSATSTMPG SNFATTNLAA SFTVRHYAGE
     VDYPVHSLVE ENGDVVSGDL MNMIKATKSD FVANLFGQEA LNTVSHPAEK TAIVQAQVSS
     KPLRMPSVSR KKHDQLRRMA SRRADRSPAP QEEEPLPGTE EAKVRRTKPT ATGLTQGAAA
     QFLSALDNIT KSLTAPNVNN YFVFCLKPND RRIANQFDSK CVRQQVQMFG IAEISQRLRT
     ADFTIFLPFG EFLGLTNADG GVVGSDREKA QLVLDSKHWP PNEARIGNTG VFLSERCWAS
     IALTGSQAAA YFGGDIGSPS RPDTPGHNPF SDSKARLVGS ADGTPGSFYG DEAKGGGYFG
     SRELDAKSDA GASAFHSGDM FRNLETKEEL AEKGNKKKVE EVDVVPVSSS RKRWLAIVYF
     LTWYLPDFAI KWIGGMKRKD VRTAWREKFA INLLIWLSCG LVVFFIIVFP ELICPKQNVY
     SAAELSAHDG KGKHSAYVAI RGQVFDLGAF MPNHYPKIIP QSSLKKYAGV DATGLFPVQV
     SALCQGKDGR VDPTVQLDYT ATNISGTAAV ISSTDANRKY HDFRYFTNDS RPDWFYEQMI
     MLKANYRKGS IGYTPQYVKT LAKKSKSIAI LNDRVYDFTT YNEGGRSVRA PPGEEVPSGV
     DTDFMDSLVV DLFTQRAGHD VTKYWNALPL DPGLRSRMQL CLDNLFFVGV TDTRNSPRCL
     FARYILLAVS ILLCSVIGFK FFAALQFGGK NVPENLDKFV ICQVPAYTED EDSLRRAIDS
     AARMRYDDKR KLLIVVCDGM IIGQGNDRPT PRIVLDILGV SETVDPEPLS FESLGEGMKQ
     HNMGKVYSGL YEVQGHIVPF MVVVKVGKPS EVSRPGNRGK RDSQMVIMRF LHRVHYNLPM
     SPLELEMHHQ IRNIIGVNPT FYEFMLQIDA DTVVAPDSAT RMVSAFLRDT RLIGVCGETS
     LSNAKSSFIT MMQVYEYYIS HNLTKAFESL FGSVTCVPGC FTMYRIRAAE TGKPLFVSKE
     IIQDYSEIRV DTLHMKNLLH LGEDRYLTTL LLKYHSKYKT KYIFHAHAWT IAPDSWKVFM
     SQRRRWINST VHNLIELIPL QQLCGFCCFS MRFVVFLDLL STVVAPVTVA YIAYLIVLLA
     TESDVVPLTA FILLGAIYGL QAIIFILRRK WEMIGWMIVY ILAMPVFSLG LPLYAFWHMD
     DFSWGNTRLV RGEHGKQILL SDEGKFGPDS IPKKKWEEYQ AELWDAQTQR DDARSELSGY
     SYGTKSYLPT GSVYGGGYND TQHLMMAPSR SASQLDMHPT PMYGGGGGHN QSRMSLAPSE
     MLGSQSNLMM PSGRSVADME MSDLTGLPTD DMLLNEIRDI LRTADLMTVT KKGIKQELER
     RFNVNLDMKR AYIGSATEAI LSGQL
//