ID   CHSB_EMENI              Reviewed;         916 AA.
AC   Q00757; C8VPK2; P87326; Q5BAA7;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Chitin synthase B;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase B;
DE   AltName: Full=Class-III chitin synthase B;
GN   Name=chsB; ORFNames=AN2523;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC 89;
RX   PubMed=7765508; DOI=10.1271/bbb.58.1828;
RA   Yanai K., Kojima N., Takaya N., Horiuchi H., Ohta A., Takagi M.;
RT   "Isolation and characterization of two chitin synthase genes from
RT   Aspergillus nidulans.";
RL   Biosci. Biotechnol. Biochem. 58:1828-1835(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FGSC 89;
RA   Tatsuno K.;
RT   "Aspergillus nidulans chitin synthase B gene.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(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. {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 III subfamily.
CC       {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; D21269; BAA04807.1; -; Genomic_DNA.
DR   EMBL; D83216; BAA11845.1; -; mRNA.
DR   EMBL; AACD01000043; EAA64628.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF87020.1; -; Genomic_DNA.
DR   PIR; JC2315; JC2315.
DR   RefSeq; XP_660127.1; XM_655035.1.
DR   AlphaFoldDB; Q00757; -.
DR   STRING; 162425.CADANIAP00009248; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblFungi; CBF87020; CBF87020; ANIA_02523.
DR   EnsemblFungi; EAA64628; EAA64628; AN2523.2.
DR   GeneID; 2874737; -.
DR   KEGG; ani:AN2523.2; -.
DR   VEuPathDB; FungiDB:AN2523; -.
DR   eggNOG; KOG2571; Eukaryota.
DR   HOGENOM; CLU_004760_0_1_1; -.
DR   InParanoid; Q00757; -.
DR   OMA; FWIFSNA; -.
DR   OrthoDB; 256142at2759; -.
DR   BRENDA; 2.4.1.16; 517.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR   GO; GO:0030428; C:cell septum; IDA:AspGD.
DR   GO; GO:0001411; C:hyphal tip; IDA:AspGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:AspGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000934; C:porous cell septum; IDA:AspGD.
DR   GO; GO:0004100; F:chitin synthase activity; IDA:AspGD.
DR   GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR   GO; GO:0030448; P:hyphal growth; IMP:AspGD.
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   2: Evidence at transcript level;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..916
FT                   /note="Chitin synthase B"
FT                   /id="PRO_0000193692"
FT   TRANSMEM        544..561
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        588..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        629..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        664..684
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        716..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        845..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        884..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        136..137
FT                   /note="AG -> RR (in Ref. 1; BAA04807 and 2; BAA11845)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   916 AA;  101882 MW;  622356DC99AA4B5E CRC64;
     MAYHGSGPQS PGEHTYDDGH QLRDLSHSNT SYEEEASHGL LSSQQSPFAG PFDDPHQQRG
     LTASPVQRPT SGYSLTESYA PDAAYHDPYS ANQSVYSGHS ENPAAAFGVP GRVASPYARS
     ETSSTEAWRQ RQAGAAGGGN GLRRYATRKV KLVQGSVLSV DYPVPSAIQN AIQAKYRNDL
     EGGSEEFTHM RYTAATCDPN EFTLHNGYNL RPAMYNRHTE LLIAITYYNE DKTLTARTLH
     GVMQNIRDIV NLKKSEFWNK GGPAWQKIVV CLVFDGIDPC DKDTLDVLAT VGIYQDGVMK
     RDVDGKETVA HIFEYTTQLS VTPNQQLIRP TDDGPSTLPP VQMMFCLKQK NSKKINSHRW
     LFNAFGRILN PEVCILLDAG TKPGPKSLLY LWEAFYNDKD LGGACGEIHA MLGKGWKKLL
     NPLVAAQNFE YKISNILDKP LESSFGYVSV LPGAFSAYRF RAIMGRPLEQ YFHGDHTLSK
     QLGKKGIEGM NIFKKNMFLA EDRILCFELV AKAGSKWHLS YVKASKGETD VPEGAPEFIS
     QRRRWLNGSF AAGIYSLMHF GRMYKSGHNI VRMFFLHLQM LYNWFSTFLT WFSLASYWLT
     TSVIMDLVGT PSSSNGYTAF PFGKTATPII NTLVKYIYLA FLLLQFILAL GNRPKGSKLS
     YLASFVAFGI IQLYVVVDAL YLVVRAFTGG APMDFNTDDG IGAFLSSFFG SSGAGIIIIA
     LAATFGLYFV ASFMYLDPWH MFTSFPAYMA VQSSYINILN VYAFSNWHDV SWGTKGSDKA
     DALPSAKTTG GKGEEAVIEE IDKPQADIDS QFEATVKRAL TPYVPPEEKE EKSLDDSYKS
     FRTRLVTLWL FSNGLLAVCI TSEGLDKFGF TNTSTERTSR FFQALLWSNA VVALIRFIGA
     TWFLGKTGLL CCFARR