ID   CHS2_RHIOL              Reviewed;         858 AA.
AC   P30595;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Chitin synthase 2;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 2;
GN   Name=CHS2;
OS   Rhizopus oligosporus (Rhizopus microsporus var. oligosporus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7765484; DOI=10.1271/bbb.58.1685;
RA   Motoyama T., Sudoh M., Horiuchi H., Ohta A., Takagi M.;
RT   "Isolation and characterization of two chitin synthase genes of Rhizopus
RT   oligosporus.";
RL   Biosci. Biotechnol. Biochem. 58:1685-1693(1994).
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. {ECO:0000305}.
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DR   EMBL; D10160; BAA01024.1; -; Genomic_DNA.
DR   PIR; JC2309; JC2309.
DR   AlphaFoldDB; P30595; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
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   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..858
FT                   /note="Chitin synthase 2"
FT                   /id="PRO_0000193712"
FT   TRANSMEM        500..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        540..560
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        586..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        621..641
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        665..685
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        799..819
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        825..845
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..99
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  96791 MW;  5B2DECFF5823408C CRC64;
     MYPEGPKPEH DQFPLQDTQF SNQPPVHRSP FEDPYPEDQP HFDKQPLLTS PAYPPTQYPT
     SPPPPNFPGS PAVQQPYPPF NNNPSPVSPG VPAYFNPAPP SPNMHYGQAP RRQPRRFKTT
     RQVKLTKGNL VLDCPVPTAY LNDVPIKDGK EFTHMRYTAA TCDPKDFASD GYTLRQPMLG
     RKTELFIVLT MYNEDEVLFA RTMHGVMKNI AHLCTRDRSR TWGPNGWEKV VVCIVSDGRN
     KINQRTLSVL ALLGVYQDGI AKNVVHGKPV TAHIYEYTTQ VSVDPNMEVK KAGSKNVVPC
     QILFCLKEKN QKKINSHRWF FQAFGPVIDP HICVLIDVGT KPGGTSIYHL WKAFDINSNI
     AGACGEIRAM AGTRGVALLN PLVAAQNFEY KMSNILDKPL ESVFGYISVL PGAFSAYRFK
     ALQNDVNGHG PLEKYFLGET QHGGDADIFT ANMYLAEDRI LCYELVAKKE AHWVLHYVSS
     SYGETDVPDK VDEFISQRRR WLNGSFFAGV YALYHWRKVW QSDHSYLRKM MFMVEDIYNT
     YNLIFSWFAL GNFYLTFFIL TKALGHGVDG STLTDPPFSP DTGETLHTVF NYIYIVLIVI
     QFIMALGNRP QGSKIAYTSS MVFFAILMVY MMFAAIWITV VGVKTVVETS GGQFIEMLEQ
     STFRNIIISL CATYVMYFVS SFMFLDPWHM FTSFIQYILL SPSYTNVLNI YAFCNTHDVS
     WGTKGDNTVA TDLGVVKAKK DGSGDLAVEV EVPVEEKDIN AAFIDAQVEL TKKIEPEKSH
     RDAKTKQEDY YRSFRTRLVL AWIISNLALV VAIANTTVID IKGKASIYLG FILWSVAGLS
     VIRFTGSTLY LIFKIFTG