CHIS_BACSU
ID CHIS_BACSU Reviewed; 277 AA.
AC O07921;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Chitosanase;
DE EC=3.2.1.132;
DE Flags: Precursor;
GN Name=csn; OrderedLocusNames=BSU26890;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9141695; DOI=10.1099/00221287-143-4-1321;
RA Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A.,
RA Mellado R.P.;
RT "A 23911 bp region of the Bacillus subtilis genome comprising genes located
RT upstream and downstream of the lev operon.";
RL Microbiology 143:1321-1326(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9308178; DOI=10.1099/00221287-143-9-2939;
RA Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J.,
RA Duesterhoeft A., Ehrlich S.D.;
RT "Sequence of the Bacillus subtilis genome region in the vicinity of the lev
RT operon reveals two new extracytoplasmic function RNA polymerase sigma
RT factors SigV and SigZ.";
RL Microbiology 143:2939-2943(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP PROTEIN SEQUENCE OF 36-45, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT dimensional protein electrophoretic study.";
RL Microbiology 146:65-75(2000).
CC -!- FUNCTION: Aids in the defense against invading fungal pathogens by
CC degrading their cell wall chitosan. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of beta-(1->4)-linkages between D-glucosamine
CC residues in a partly acetylated chitosan.; EC=3.2.1.132;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10658653}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 46 family. {ECO:0000305}.
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DR EMBL; X92868; CAA63455.1; -; Genomic_DNA.
DR EMBL; U93875; AAB80882.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14630.1; -; Genomic_DNA.
DR PIR; C69608; C69608.
DR RefSeq; NP_390566.1; NC_000964.3.
DR RefSeq; WP_003229851.1; NZ_JNCM01000036.1.
DR PDB; 7C6C; X-ray; 1.26 A; A=36-277.
DR PDB; 7C6D; X-ray; 1.45 A; A=36-277.
DR PDBsum; 7C6C; -.
DR PDBsum; 7C6D; -.
DR AlphaFoldDB; O07921; -.
DR SMR; O07921; -.
DR STRING; 224308.BSU26890; -.
DR CAZy; GH46; Glycoside Hydrolase Family 46.
DR PaxDb; O07921; -.
DR PRIDE; O07921; -.
DR EnsemblBacteria; CAB14630; CAB14630; BSU_26890.
DR GeneID; 936802; -.
DR KEGG; bsu:BSU26890; -.
DR PATRIC; fig|224308.179.peg.2921; -.
DR eggNOG; COG3409; Bacteria.
DR InParanoid; O07921; -.
DR OMA; AQNDERD; -.
DR PhylomeDB; O07921; -.
DR BioCyc; BSUB:BSU26890-MON; -.
DR BioCyc; MetaCyc:BSU26890-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016977; F:chitosanase activity; IDA:CACAO.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00978; chitosanase_GH46; 1.
DR Gene3D; 3.30.386.10; -; 1.
DR InterPro; IPR000400; Glyco_hydro_46.
DR InterPro; IPR023099; Glyco_hydro_46_N.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF01374; Glyco_hydro_46; 1.
DR PIRSF; PIRSF036551; Chitosanase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS60000; CHITOSANASE_46_80; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:10658653"
FT CHAIN 36..277
FT /note="Chitosanase"
FT /id="PRO_0000012207"
FT ACT_SITE 54
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10070"
FT ACT_SITE 70
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:7C6C"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:7C6C"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:7C6C"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:7C6C"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:7C6C"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:7C6C"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:7C6C"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 212..228
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:7C6C"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:7C6C"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:7C6C"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:7C6C"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:7C6C"
SQ SEQUENCE 277 AA; 31497 MW; 8C17C156AF27F781 CRC64;
MKISMQKADF WKKAAISLLV FTMFFTLMMS ETVFAAGLNK DQKRRAEQLT SIFENGTTEI
QYGYVERLDD GRGYTCGRAG FTTATGDALE VVEVYTKAVP NNKLKKYLPE LRRLAKEESD
DTSNLKGFAS AWKSLANDKE FRAAQDKVND HLYYQPAMKR SDNAGLKTAL ARAVMYDTVI
QHGDGDDPDS FYALIKRTNK KAGGSPKDGI DEKKWLNKFL DVRYDDLMNP ANHDTRDEWR
ESVARVDVLR SIAKENNYNL NGPIHVRSNE YGNFVIK
