PDAB_BACSU
ID PDAB_BACSU Reviewed; 254 AA.
AC P50865;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable polysaccharide deacetylase PdaB;
DE EC=3.-.-.-;
DE Flags: Precursor;
GN Name=pdaB; Synonyms=ybaN, ybxG; OrderedLocusNames=BSU01570;
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=8969501; DOI=10.1099/13500872-142-11-3039;
RA Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA Kawamura F., Yoshikawa H., Takahashi H.;
RT "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT subtilis chromosome.";
RL Microbiology 142:3039-3046(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 156-254.
RC STRAIN=168 / JH642;
RX PubMed=8576055; DOI=10.1128/jb.178.4.1178-1186.1996;
RA Dartois V., Djavakhishvili T., Hoch J.A.;
RT "Identification of a membrane protein involved in activation of the KinB
RT pathway to sporulation in Bacillus subtilis.";
RL J. Bacteriol. 178:1178-1186(1996).
RN [4]
RP ROLE IN SPORULATION.
RC STRAIN=168;
RX PubMed=15598884; DOI=10.1093/jb/mvh151;
RA Fukushima T., Tanabe T., Yamamoto H., Hosoya S., Sato T., Yoshikawa H.,
RA Sekiguchi J.;
RT "Characterization of a polysaccharide deacetylase gene homologue (pdaB) on
RT sporulation of Bacillus subtilis.";
RL J. Biochem. 136:283-291(2004).
CC -!- FUNCTION: Necessary to maintain spores after the late stage of
CC sporulation. Might be involved in cortex formation.
CC {ECO:0000269|PubMed:15598884}.
CC -!- ACTIVITY REGULATION: Negatively regulated by SpoIIID.
CC -!- SUBCELLULAR LOCATION: Forespore. Note=Produced in the mother cell
CC compartment and transported into the forespore.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; D64126; BAA10997.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11933.1; -; Genomic_DNA.
DR EMBL; U23797; AAC44001.1; -; Genomic_DNA.
DR PIR; B69743; B69743.
DR RefSeq; NP_388038.1; NC_000964.3.
DR RefSeq; WP_003235130.1; NZ_JNCM01000029.1.
DR AlphaFoldDB; P50865; -.
DR SMR; P50865; -.
DR STRING; 224308.BSU01570; -.
DR PaxDb; P50865; -.
DR PRIDE; P50865; -.
DR EnsemblBacteria; CAB11933; CAB11933; BSU_01570.
DR GeneID; 938911; -.
DR KEGG; bsu:BSU01570; -.
DR PATRIC; fig|224308.179.peg.161; -.
DR eggNOG; COG0726; Bacteria.
DR InParanoid; P50865; -.
DR OMA; VLFHNNA; -.
DR PhylomeDB; P50865; -.
DR BioCyc; BSUB:BSU01570-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0042763; C:intracellular immature spore; IEA:UniProtKB-SubCell.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR014132; PdaB-like.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR TIGRFAMs; TIGR02764; spore_ybaN_pdaB; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome; Signal; Sporulation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..254
FT /note="Probable polysaccharide deacetylase PdaB"
FT /id="PRO_0000024843"
FT DOMAIN 57..237
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
SQ SEQUENCE 254 AA; 28323 MW; BF1F54E2AD6438EB CRC64;
MNHFYVWHIK RVKQLIIILI AAFAAASFFY IQRAVPLPVF STDTGPKAIY KGETDSKDIS
LTFDISWGDE RAEPILNTLK ANGIKNATFF LSASWAERHP DTVARIVKDG HQIGSMGYAY
KNYANLESSE IKKDMNRAQT AFEKLGVKDI QLLRPPTGQF NKNVLKVAKQ YNYTVVHYSV
NSQDWTNPGV EKIIDNVTKQ VSGGDIILLH ASDSAKQTEE ALPDIIHQLK EKGLKNVTVG
DLIANSDAKS AEVK
