PDUU_CITFR
ID PDUU_CITFR Reviewed; 116 AA.
AC P0DUV8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Bacterial microcompartment shell protein PduU {ECO:0000303|PubMed:18332146};
DE AltName: Full=Bacterial microcompartment protein homohexamer {ECO:0000305};
DE Short=BMC-H {ECO:0000305};
DE AltName: Full=Propanediol utilization protein PduU;
GN Name=pduU {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, AND PATHWAY.
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, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
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: A minor shell protein of the bacterial microcompartment (BMC)
CC dedicated to 1,2-propanediol (1,2-PD) degradation. May selectively
CC transport specific metabolites (By similarity). Not absolutely required
CC to make artificial BMCs (PubMed:20417607). Proteins such as this one
CC with circularly permuted BMC domains may play a key role in conferring
CC heterogeneity and flexibility in this BMC (Probable).
CC {ECO:0000250|UniProtKB:P0A1D1, ECO:0000269|PubMed:20417607,
CC ECO:0000305}.
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 bacterial microcompartments (BMC) in its cytoplasm.
CC Overexpression of this protein leads to multiple smaller structures
CC which appear to clump together in the cytoplasm.
CC {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: Homohexamer with a central pore lined by a beta-barrel.
CC Hexamers pack into a loose array. Interacts with PduV, probably via the
CC beta-barrel, which is predicted by modeling to be on the exterior of
CC the BMC (By similarity). Interacts with shell protein PduA
CC (PubMed:20417607). {ECO:0000250|UniProtKB:P0A1D1,
CC ECO:0000269|PubMed:20417607}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:20417607}.
CC -!- DOMAIN: One side of the hexamer is concave which is lined by
CC hydrophobic residues, the other side has a slightly protruding, 6-
CC stranded beta-barrel. {ECO:0000250|UniProtKB:A0A0E2IV13}.
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 EutS/PduU family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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DR EMBL; AM498294; CAM57300.1; -; Genomic_DNA.
DR UniPathway; UPA00621; -.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07046; BMC_PduU-EutS; 1.
DR Gene3D; 3.30.70.1710; -; 1.
DR InterPro; IPR044870; BMC_CP.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR009307; EutS/PduU/CutR.
DR PANTHER; PTHR40449; PTHR40449; 1.
DR Pfam; PF00936; BMC; 1.
DR PIRSF; PIRSF012296; EutS_PduU; 1.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; SSF143414; 1.
DR PROSITE; PS51931; BMC_CP; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Transport.
FT CHAIN 1..116
FT /note="Bacterial microcompartment shell protein PduU"
FT /id="PRO_0000454250"
FT DOMAIN 9..108
FT /note="BMC circularly permuted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
SQ SEQUENCE 116 AA; 12484 MW; 38665793A5374519 CRC64;
MERQPTTDRM IQEYVPGKQV TLAHLIANPG KDLFKKLGLP ESVSAIGILT ITPSEASIIA
CDIATKSGAV EIGFLDRFTG AVVLTGDVSA VEYALKQVTR TLGEMMRFTA CPITRT
