ID   CHSA_AMPQU              Reviewed;         910 AA.
AC   Q12564;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Chitin synthase A;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase A;
DE   AltName: Full=Class-I chitin synthase A;
GN   Name=CHSA;
OS   Ampelomyces quisqualis (Powdery mildew agent).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Ampelomyces.
OX   NCBI_TaxID=50730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AQ10;
RX   PubMed=8626074; DOI=10.1016/0378-1119(95)00722-9;
RA   Weiss N., Sztejnberg A., Yarden O.;
RT   "The chsA gene, encoding a class-I chitin synthase from Ampelomyces
RT   quisqualis.";
RL   Gene 168:99-102(1996).
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. {ECO:0000305}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. Class I subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X86802; CAA60497.1; -; Genomic_DNA.
DR   PIR; JC4609; JC4609.
DR   AlphaFoldDB; Q12564; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PRIDE; Q12564; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006031; P:chitin biosynthetic process; IEA:InterPro.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR004834; Chitin_synth_fun.
DR   InterPro; IPR013616; Chitin_synth_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF01644; Chitin_synth_1; 1.
DR   Pfam; PF08407; Chitin_synth_1N; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..910
FT                   /note="Chitin synthase A"
FT                   /id="PRO_0000193679"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        583..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        620..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        655..675
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        701..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        730..750
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        828..848
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        876..896
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          56..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   910 AA;  103013 MW;  F8F1DB135F2138F9 CRC64;
     MARRQGPSRS PWAPTQRRRL ATDCPCSRVY VLAHTAAAVA NSEQYSVENI PYAGGNYHDD
     YDPRPGGRRH DSDYSLDPNA HHDAYYSQPY DPAPHDASPG GAYGTQPDHY WQDDDVGRPM
     IQGANAYGPD PHDPDRDPHP DDPFHDEPAP TPTPAPIKRW KTVKEVQLFK GNLVLDCPIP
     PRLLNQVPHA QPPERDEFTH MRYSAATCDP ADFDAERFTL RQKLFAKPRH TELFIVITMY
     NEEDELFART MTGVIKNIEY MNSRTNSKTW GKDAWKKIVV CVVSDGRAKI NPRTRAVLAA
     LGVYQDGIAK QQVNGKDVTA HIYEYTTQMT LDIKKGVVGV KKGNTPVQML FCLKEKNQKK
     INSHRWFFQA FGQVLDPNIC VLIDAGTKPG KDSVYQLWKA FDLEPMCAGA CGEIKAMLVH
     GKKLLNPLVA TQNFEYKMSN ILDKPLESAF GFITVLPGAF SAYRYVALQN DKAGQGPLEK
     YFAGEKMHGA NAGIFTANMY LAEDRILCFE LVSKRNCHWI LQYVKSATGE TDVPTTMAEF
     ISQRRRWLNG SFFAAVYALA HSFDIFRSDH SFLRKTMFLV EFVYQTISML FAWFALGNFF
     LVFRILTASL QNELGTAGKV LFIVFEWLYI AVLITCFILS LGNRPQGSNK WYMSMVYFWG
     VIMAYLMFAS IFITVRSIQS QIRNNGGFNA SDLLKDKIFA TLIISLLSTY VMWLVVSIIF
     LDPWHMFTSF IQYLLMTPTY INILNVYAFC NTHDITWGTK GDDKPEKLPS VTTKADGKAD
     IHAPTDDADL NTQYETELHV FSTKWKEEKK VPSPGEKQED YYRGFRSGVV LFWMFCNLAL
     TALVLQAGGL ELTVSDPDEA QEKQNQASTI YLAVVLYSVA GLAAFRFIGA MWFLVVRMVS
     ATCRFTSPIY