PDUJ_CITFR
ID PDUJ_CITFR Reviewed; 91 AA.
AC P0DUV5;
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 PduJ {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 PduJ;
GN Name=pduJ {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, PATHWAY, AND SUBCELLULAR LOCATION.
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.
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: One of the major shell proteins of the bacterial
CC microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD)
CC degradation (Probable). At least one of PduA or PduJ is required for
CC BMC assembly; it must be encoded as the first gene in the pdu operon.
CC Required for structural integrity of BMCs and to mitigate
CC propionaldehyde toxicity, probably joins facets responsible for BMC
CC closure. Probably the hub for binding multiple enzymes to the interior
CC of the BMC (By similarity). {ECO:0000250|UniProtKB:H9L478,
CC ECO:0000305|PubMed:20417607}.
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-PD with the appearance of BMCs
CC in its cytoplasm. Overexpression of this protein leads to an internal
CC structure with a whorled architecture. {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. Interacts with PduP, which
CC targets PduP to the BMC (By similarity). Interacts with shell protein
CC PduA (PubMed:20417607). {ECO:0000250|UniProtKB:H9L478,
CC ECO:0000269|PubMed:20417607}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:18332146, ECO:0000269|PubMed:20417607}.
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 bacterial microcompartments protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01278}.
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DR EMBL; AM498294; CAM57290.1; -; 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 Gene3D; 3.30.70.1710; -; 1.
DR InterPro; IPR020808; Bact_microcomp_CS.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR044872; CcmK/CsoS1_BMC.
DR Pfam; PF00936; BMC; 1.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; SSF143414; 1.
DR PROSITE; PS01139; BMC_1; 1.
DR PROSITE; PS51930; BMC_2; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Transport.
FT CHAIN 1..91
FT /note="Bacterial microcompartment shell protein PduJ"
FT /id="PRO_0000454251"
FT DOMAIN 4..88
FT /note="BMC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
SQ SEQUENCE 91 AA; 9053 MW; A02EF5D2267F22DF CRC64;
MNNALGLVET KGLVGAIEAA DAMVKSANVQ LVGYEKIGSG LITVMVRGDV GAVKAAVDAG
SAAASAVGEV KSCHVIPRPH SDVEAILPKS A
