PDUT_CITFR
ID PDUT_CITFR Reviewed; 184 AA.
AC P0DUV7;
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 PduT {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 PduT;
GN Name=pduT {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, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-38; CYS-108 AND CYS-136.
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, 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 INTERACTION WITH PDUS.
RX PubMed=21103360; DOI=10.1371/journal.pone.0014009;
RA Parsons J.B., Lawrence A.D., McLean K.J., Munro A.W., Rigby S.E.,
RA Warren M.J.;
RT "Characterisation of PduS, the pdu metabolosome corrin reductase, and
RT evidence of substructural organisation within the bacterial
RT microcompartment.";
RL PLoS ONE 5:e14009-e14009(2010).
RN [4] {ECO:0007744|PDB:3PAC}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), COFACTOR, AND SUBUNIT.
RX PubMed=21245529; DOI=10.1107/s0907444910050201;
RA Pang A., Warren M.J., Pickersgill R.W.;
RT "Structure of PduT, a trimeric bacterial microcompartment protein with a
RT 4Fe-4S cluster-binding site.";
RL Acta Crystallogr. D 67:91-96(2011).
CC -!- FUNCTION: A minor shell protein of the bacterial microcompartment (BMC)
CC dedicated to 1,2-propanediol (1,2-PD) degradation. Overexpression of
CC this protein leads to cells with either deposits or having lamina-like
CC structures in the cytoplasm (PubMed:18332146). Not absolutely required
CC to make artificial BMCs (PubMed:20417607). May selectively transport
CC specific metabolites (By similarity). {ECO:0000250|UniProtKB:Q9XDM8,
CC ECO:0000269|PubMed:18332146, ECO:0000269|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-propanediol (1,2-PD) with the
CC appearance of bacterial microcompartments (BMC) in its 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:18332146, ECO:0000305|PubMed:21245529};
CC Note=Seems to be bound by a single Cys residue from each of 4 subunits
CC (Probable). 3 ligands are provided by each trimer, the fourth ligand
CC could potentially bind another protein (Probable). The cluster is
CC accessible from both sides of the trimer (PubMed:21245529).
CC {ECO:0000269|PubMed:21245529, ECO:0000305|PubMed:18332146,
CC ECO:0000305|PubMed:21245529};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +99 mV. {ECO:0000269|PubMed:18332146};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000269|PubMed:18332146}.
CC -!- SUBUNIT: Homotrimerizes to form a pseudohexamer with a large central
CC pore, which is probably the binding site for the [4Fe-4S] center
CC (PubMed:21245529). Interacts with PduS (PubMed:21103360). Originally
CC suggested to be a homotetramer; this is incorrect (Probable).
CC {ECO:0000269|PubMed:21103360, ECO:0000269|PubMed:21245529,
CC ECO:0000305|PubMed:18332146}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:20417607, ECO:0000305|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 {ECO:0000269|PubMed:20417607}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01278}.
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DR EMBL; AM498294; CAM57299.1; -; Genomic_DNA.
DR PDB; 3PAC; X-ray; 1.86 A; A=1-184.
DR PDBsum; 3PAC; -.
DR UniPathway; UPA00621; -.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.1710; -; 2.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR044872; CcmK/CsoS1_BMC.
DR InterPro; IPR011238; Organelle_shell_prot_PduT.
DR Pfam; PF00936; BMC; 2.
DR PIRSF; PIRSF034834; PduT; 1.
DR SMART; SM00877; BMC; 2.
DR SUPFAM; SSF143414; SSF143414; 2.
DR PROSITE; PS51930; BMC_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Bacterial microcompartment; Iron; Iron-sulfur;
KW Metal-binding; Transport.
FT CHAIN 1..184
FT /note="Bacterial microcompartment shell protein PduT"
FT /id="PRO_0000454255"
FT DOMAIN 4..86
FT /note="BMC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT DOMAIN 96..182
FT /note="BMC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:18332146"
FT MUTAGEN 38
FT /note="C->A: Loss of 4Fe-4S center."
FT /evidence="ECO:0000269|PubMed:18332146"
FT MUTAGEN 108
FT /note="C->A: Retains 4Fe-4S center."
FT /evidence="ECO:0000269|PubMed:18332146"
FT MUTAGEN 136
FT /note="C->A: Retains 4Fe-4S center."
FT /evidence="ECO:0000269|PubMed:18332146"
SQ SEQUENCE 184 AA; 19038 MW; D9DB4A5EC2232CAC CRC64;
MSQAIGILEL TSIAKGMEAG DAMLKSANVN LLVSKTICPG KFLLMLGGDV GAVQQAIATG
TSLAGDMLVD SLVLPNIHAS VLPAISGLNS VDKRQAVGIV ETWSVAACIC AADRAVKASN
VTLVRVHMAF GIGGKCYMVV AGDVSDVNNA VTVASESAGE KGLLVYRSVI PRPHESMWRQ
MVEG
