PDUB_CITFR
ID PDUB_CITFR Reviewed; 270 AA.
AC B1VB63;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Bacterial microcompartment shell protein PduB {ECO:0000303|PubMed:18332146};
DE AltName: Full=Bacterial microcompartment protein homotrimer {ECO:0000305};
DE Short=BMC-T {ECO:0000305};
DE AltName: Full=Propanediol utilization protein PduB;
GN Name=pduB {ECO:0000303|PubMed:18332146};
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, IDENTIFICATION BY MASS
RP SPECTROMETRY, PDUB AND PDUB' ISOFORMS, PATHWAY, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF MET-38.
RX PubMed=18332146; DOI=10.1074/jbc.m709214200;
RA Parsons J.B., Dinesh S.D., Deery E., Leech H.K., Brindley A.A., Heldt D.,
RA Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., Bleloch A.,
RA McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., Prentice M.B.;
RT "Biochemical and Structural Insights into Bacterial Organelle Form and
RT Biogenesis.";
RL J. Biol. Chem. 283:14366-14375(2008).
RN [2]
RP FUNCTION, INTERACTION WITH PDUA, SUBUNIT, SUBCELLULAR LOCATION, AND
RP BIOTECHNOLOGY (ARTIFICIAL BMCS).
RX PubMed=20417607; DOI=10.1016/j.molcel.2010.04.008;
RA Parsons J.B., Frank S., Bhella D., Liang M., Prentice M.B., Mulvihill D.P.,
RA Warren M.J.;
RT "Synthesis of empty bacterial microcompartments, directed organelle protein
RT incorporation, and evidence of filament-associated organelle movement.";
RL Mol. Cell 38:305-315(2010).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=24933391; DOI=10.1021/sb4001118;
RA Lawrence A.D., Frank S., Newnham S., Lee M.J., Brown I.R., Xue W.F.,
RA Rowe M.L., Mulvihill D.P., Prentice M.B., Howard M.J., Warren M.J.;
RT "Solution structure of a bacterial microcompartment targeting peptide and
RT its application in the construction of an ethanol bioreactor.";
RL ACS Synth. Biol. 3:454-465(2014).
CC -!- FUNCTION: The two proteins produced are among the major shell proteins
CC of the bacterial microcompartment (BMC) shell dedicated to 1,2-
CC propanediol (1,2-PD) degradation. Overexpression of the gene gives
CC large amorphous intracellular structures; when only PduB is
CC overexpressed large circular bodies are observed which contain
CC concentric rings, whereas with PduB' overexpression internal bodies
CC with regular straight-lined structures were generated
CC (PubMed:18332146). The N-terminus of the long form (PduB) is required
CC for correct formation of BMCs. May play a major role in binding the
CC enzyme contents to the shell (By similarity).
CC {ECO:0000250|UniProtKB:P37449, ECO:0000269|PubMed:18332146}.
CC -!- FUNCTION: Expression of a cosmid containing the full 21-gene pdu operon
CC in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the
CC appearance of BMCs in its cytoplasm. {ECO:0000269|PubMed:18332146}.
CC -!- FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC)
CC concentrates low levels of 1,2-PD catabolic enzymes, concentrates
CC volatile reaction intermediates thus enhancing pathway flux and keeps
CC the level of toxic, mutagenic propionaldehyde low.
CC {ECO:0000305|PubMed:20417607}.
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000269|PubMed:18332146}.
CC -!- SUBUNIT: Homotrimerizes to form a pseudohexamer with a central pore.
CC The trimers pack into an array (By similarity). Both forms interact
CC with shell protein PduA (PubMed:20417607).
CC {ECO:0000250|UniProtKB:A5VMB3, ECO:0000269|PubMed:20417607}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:18332146, ECO:0000269|PubMed:20417607}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=PduB;
CC IsoId=B1VB63-1; Sequence=Displayed;
CC Name=PduB';
CC IsoId=B1VB63-2; Sequence=VSP_061271;
CC -!- DOMAIN: Has 2 BMC domains which can evolve independently of each other.
CC {ECO:0000305}.
CC -!- PTM: In purified BMCs seen as a 30.0 kDa and 25.0 kDa form; the smaller
CC form is called PduB'. {ECO:0000269|PubMed:18332146}.
CC -!- DISRUPTION PHENOTYPE: When the whole pdu operon except this gene is
CC expressed in E.coli no BMCs are made; with the whole operon many BMCs
CC are produced in E.coli. {ECO:0000269|PubMed:18332146}.
CC -!- BIOTECHNOLOGY: Artificial BMCs can be made in E.coli by expressing
CC pduA-pduB/B'-pduJ-pduK-pduN-pduU-pduT (in this order); pduT and pduU
CC are optional, while pduA, pduB/B', pduJ, pduK and pduN are essential. A
CC construct with the reversed gene order does not make BMCs
CC (PubMed:20417607). Ethanogenic BMCs can be made in E.coli by targeting
CC pyruvate decarboxylase (pdc) and alcohol dehydrogenase (adh) to them.
CC PduP(1-18)-Pdc and PduD(1-18)-Adh strains targeted to the BMC (PduA,
CC PduB, PduJ, PduK, PduN, PduU) make significantly more ethanol than
CC strains where Pdc and Adh are not targeted to the BMC
CC (PubMed:24933391). {ECO:0000269|PubMed:20417607,
CC ECO:0000269|PubMed:24933391}.
CC -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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DR EMBL; AM498294; CAM57284.1; -; Genomic_DNA.
DR RefSeq; WP_016153528.1; NZ_LIDR01000043.1.
DR GeneID; 66273922; -.
DR UniPathway; UPA00621; -.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.1710; -; 2.
DR InterPro; IPR044870; BMC_CP.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR009193; EutL_PduB.
DR InterPro; IPR030984; PduB.
DR Pfam; PF00936; BMC; 2.
DR PIRSF; PIRSF012290; EutL_PduB; 1.
DR SMART; SM00877; BMC; 2.
DR SUPFAM; SSF143414; SSF143414; 2.
DR TIGRFAMs; TIGR04501; microcomp_PduB; 1.
DR PROSITE; PS51931; BMC_CP; 2.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Bacterial microcompartment.
FT CHAIN 1..270
FT /note="Bacterial microcompartment shell protein PduB"
FT /id="PRO_0000454247"
FT DOMAIN 47..152
FT /note="BMC circularly permuted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT DOMAIN 154..262
FT /note="BMC circularly permuted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform PduB')"
FT /evidence="ECO:0000269|PubMed:18332146"
FT /id="VSP_061271"
FT MUTAGEN 38
FT /note="M->A: PduB' no longer produced in E.coli."
FT /evidence="ECO:0000269|PubMed:18332146"
SQ SEQUENCE 270 AA; 28022 MW; 8B0A46B03E5943F1 CRC64;
MSSNELVDQI MAQVIARVAT PEQQAIPENN PPTRETAMAE KSCSLTEFVG TAIGDTVGLV
IANVDSALLD AMKLEKRYRS IGILGARTGA GPHIMAADEA VKATNTEVVS IELPRDTKGG
AGHGSLIILG GNDVSDVKRG IEVALKELDR TFGDVYANEA GHIEMQYTAR ASYALEKAFG
APIGRACGVI VGAPASVGVL MADTALKSAN VEVVAYSSPA HGTSFSNEAI LVISGDSGAV
RQAVISAREI GKTVLGTLGS EPKNDRPSYI
