BESA_BACSU
ID BESA_BACSU Reviewed; 289 AA.
AC O32102;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ferri-bacillibactin esterase BesA;
DE EC=3.1.-.-;
DE AltName: Full=Bacillibactin trilactone hydrolase;
GN Name=besA; Synonyms=yuiI; OrderedLocusNames=BSU32010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP INDUCTION BY FUR.
RC STRAIN=168;
RX PubMed=12354229; DOI=10.1046/j.1365-2958.2002.03113.x;
RA Baichoo N., Wang T., Ye R., Helmann J.D.;
RT "Global analysis of the Bacillus subtilis Fur regulon and the iron
RT starvation stimulon.";
RL Mol. Microbiol. 45:1613-1629(2002).
RN [3]
RP FUNCTION AS AN ESTERASE, KINETIC PARAMETERS, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 21332 / IAM 1213;
RX PubMed=16889643; DOI=10.1111/j.1365-2958.2006.05321.x;
RA Miethke M., Klotz O., Linne U., May J.J., Beckering C.L., Marahiel M.A.;
RT "Ferri-bacillibactin uptake and hydrolysis in Bacillus subtilis.";
RL Mol. Microbiol. 61:1413-1427(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of the trilactone cycle of ferri-
CC bacillibactin (ferri-BB) complex, leading to the formation of
CC bacillibactin monomers and to cytosolic iron release, thus making iron
CC available for metabolic use. Can also hydrolyze bacillibactin (BB),
CC however the catalytic efficiency for ferri-BB hydrolysis is much higher
CC than for BB. {ECO:0000269|PubMed:16889643}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 uM for ferri-bacillibactin complex
CC {ECO:0000269|PubMed:16889643};
CC KM=24.4 uM for bacillibactin {ECO:0000269|PubMed:16889643};
CC KM=221 uM for enterobactin {ECO:0000269|PubMed:16889643};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16889643}.
CC -!- INDUCTION: Repressed by fur in the presence of iron.
CC {ECO:0000269|PubMed:12354229}.
CC -!- DISRUPTION PHENOTYPE: Impaired growth during iron limitation conditions
CC and a strong accumulation of intracellular ferri-bacillibactin.
CC {ECO:0000269|PubMed:16889643}.
CC -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15191.2; -; Genomic_DNA.
DR RefSeq; NP_391081.2; NC_000964.3.
DR RefSeq; WP_003228740.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32102; -.
DR SMR; O32102; -.
DR STRING; 224308.BSU32010; -.
DR ESTHER; bacsu-YUII; A85-IroE-IroD-Fes-Yiel.
DR PaxDb; O32102; -.
DR PRIDE; O32102; -.
DR EnsemblBacteria; CAB15191; CAB15191; BSU_32010.
DR GeneID; 936592; -.
DR KEGG; bsu:BSU32010; -.
DR PATRIC; fig|224308.179.peg.3467; -.
DR eggNOG; COG2819; Bacteria.
DR InParanoid; O32102; -.
DR OMA; KPWVEAN; -.
DR PhylomeDB; O32102; -.
DR BioCyc; BSUB:BSU32010-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..289
FT /note="Ferri-bacillibactin esterase BesA"
FT /id="PRO_0000389644"
FT ACT_SITE 163
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 263
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 289 AA; 32439 MW; 44780F01199BC510 CRC64;
MKEQTTDRTN GGTSNAFTIP GTEVRMMSSR NENRTYHIFI SKPSTPPPPA GYPVIYLLDA
NSVFGTMTEA VRIQGRRPEK TGVIPAVIVG IGYETAEPFS SARHRDFTMP TAQSKLPERP
DGREWPEHGG AEGFFRFIEE DLKPEIERDY QIDKKRQTIF GHSLGGLFVL QVLLTKPDAF
QTYIAGSPSI HWNKPFILKK TDHFVSLTKK NNQPINILLA AGELEQHHKS RMNDNARELY
ERLAVLSEQG IRAEFCEFSG EGHISVLPVL VSRALRFALH PDGPHLSMG
