XYNB_BACSU
ID XYNB_BACSU Reviewed; 533 AA.
AC P94489; Q796H4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Beta-xylosidase;
DE EC=3.2.1.37;
DE AltName: Full=1,4-beta-D-xylan xylohydrolase;
DE AltName: Full=Xylan 1,4-beta-xylosidase;
GN Name=xynB; OrderedLocusNames=BSU17580;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.;
RT "Sequencing of a 26 kb region of the Bacillus subtilis genome downstream of
RT spoVJ.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP SEQUENCE REVISION TO 517.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=6413490; DOI=10.1128/jb.156.1.257-263.1983;
RA Roncero M.I.;
RT "Genes controlling xylan utilization by Bacillus subtilis.";
RL J. Bacteriol. 156:257-263(1983).
RN [5]
RP INDUCTION.
RX PubMed=9973552; DOI=10.1006/jmbi.1998.2492;
RA Galinier A., Deutscher J., Martin-Verstraete I.;
RT "Phosphorylation of either crh or HPr mediates binding of CcpA to the
RT bacillus subtilis xyn cre and catabolite repression of the xyn operon.";
RL J. Mol. Biol. 286:307-314(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of beta-1,4-xylosidase from Bacillus subtilis.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC Evidence={ECO:0000269|PubMed:6413490};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:6413490};
CC Peripheral membrane protein {ECO:0000305|PubMed:6413490}.
CC -!- INDUCTION: Up-regulated by xylose. Subject to carbon catabolite
CC repression (CCR). {ECO:0000269|PubMed:9973552}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR EMBL; U66480; AAB41091.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13642.2; -; Genomic_DNA.
DR PIR; G69735; G69735.
DR RefSeq; NP_389640.2; NC_000964.3.
DR RefSeq; WP_003245202.1; NZ_JNCM01000035.1.
DR PDB; 1YIF; X-ray; 1.80 A; A/B/C/D=1-533.
DR PDBsum; 1YIF; -.
DR AlphaFoldDB; P94489; -.
DR SMR; P94489; -.
DR STRING; 224308.BSU17580; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR PaxDb; P94489; -.
DR PRIDE; P94489; -.
DR DNASU; 939472; -.
DR EnsemblBacteria; CAB13642; CAB13642; BSU_17580.
DR GeneID; 939472; -.
DR KEGG; bsu:BSU17580; -.
DR PATRIC; fig|224308.179.peg.1908; -.
DR eggNOG; COG3507; Bacteria.
DR InParanoid; P94489; -.
DR OMA; LVNYYNT; -.
DR PhylomeDB; P94489; -.
DR BioCyc; BSUB:BSU17580-MON; -.
DR BRENDA; 3.2.1.37; 658.
DR EvolutionaryTrace; P94489; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell membrane; Glycosidase;
KW Hydrolase; Membrane; Polysaccharide degradation; Reference proteome;
KW Xylan degradation.
FT CHAIN 1..533
FT /note="Beta-xylosidase"
FT /id="PRO_0000360522"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT SITE 127
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT CONFLICT 517
FT /note="S -> G (in Ref. 1; AAB41091)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 38..52
FT /evidence="ECO:0007829|PDB:1YIF"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:1YIF"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 241..253
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:1YIF"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 287..297
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:1YIF"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 387..396
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 404..413
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 416..425
FT /evidence="ECO:0007829|PDB:1YIF"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 429..438
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 469..479
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 482..489
FT /evidence="ECO:0007829|PDB:1YIF"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:1YIF"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 508..515
FT /evidence="ECO:0007829|PDB:1YIF"
FT STRAND 522..532
FT /evidence="ECO:0007829|PDB:1YIF"
SQ SEQUENCE 533 AA; 61366 MW; 087286AACE705F1D CRC64;
MKITNPVLKG FNPDPSICRA GEDYYIAVST FEWFPGVQIH HSKDLVNWHL VAHPLQRVSQ
LDMKGNPNSG GVWAPCLSYS DGKFWLIYTD VKVVDGAWKD CHNYLVTCET INGDWSEPIK
LNSSGFDASL FHDTDGKKYL LNMLWDHRID RHSFGGIVIQ EYSDKEQKLI GKPKVIFEGT
DRKLTEAPHL YHIGNYYYLL TAEGGTRYEH AATIARSANI EGPYEVHPDN PILTSWHDPG
NPLQKCGHAS IVQTHTDEWY LAHLTGRPIH PDDDSIFQQR GYCPLGRETA IQKLYWKDEW
PYVVGGKEGS LEVDAPSIPE TIFEATYPEV DEFEDSTLNI NFQTLRIPFT NELGSLTQAP
NHLRLFGHES LTSTFTQAFV ARRWQSLHFE AETAVEFYPE NFQQAAGLVN YYNTENWTAL
QVTHDEELGR ILELTICDNF SFSQPLNNKI VIPREVKYVY LRVNIEKDKY YYFYSFNKED
WHKIDIALES KKLSDDYIRG GGFFTGAFVG MQCQDTSGNH IPADFRYFRY KEK
