ID   PDUK_CITFR              Reviewed;         156 AA.
AC   B1VB70;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Bacterial microcompartment shell protein PduK {ECO:0000303|PubMed:18332146};
DE   AltName: Full=Propanediol utilization protein PduK;
GN   Name=pduK {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 AND PDUM, 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   INTERACTION WITH PDUP, AND 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.
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-propanediol (1,2-PD) with the
CC       appearance of bacterial microcompartments (BMC) in its cytoplasm.
CC       Overexpression of this protein leads to the appearance of a single
CC       large aggregate complex 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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q9XDN6};
CC       Note=Might bind an [Fe-S] cluster in vivo.
CC       {ECO:0000250|UniProtKB:Q9XDN6};
CC   -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC       {ECO:0000269|PubMed:18332146}.
CC   -!- SUBUNIT: Interacts with shell protein PduA and assembly protein PduM
CC       (PubMed:20417607). Interacts with PduP, probably with its first 18
CC       residues (PubMed:24933391). {ECO:0000269|PubMed:20417607,
CC       ECO:0000269|PubMed:24933391}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {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; CAM57291.1; -; Genomic_DNA.
DR   SMR; B1VB70; -.
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; 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; PS51930; BMC_2; 1.
PE   1: Evidence at protein level;
KW   Bacterial microcompartment; Iron.
FT   CHAIN           1..156
FT                   /note="Bacterial microcompartment shell protein PduK"
FT                   /id="PRO_0000454253"
FT   DOMAIN          4..89
FT                   /note="BMC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT   REGION          81..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   156 AA;  16122 MW;  A2510DC49A333135 CRC64;
     MKQSLGLLEV SGLALAISCA DVMAKAASIT LVGLEKTNGS GWMVIKIIGD VASVQAAIST
     GVSFADQRDG LVAHKVISRP GDGILSHSVT PESESEPAPA PTPVVPHEEI PEDHAAPEAP
     QDAELISCNL CLDPACPRQK GEPRSLCLHS GKRGEA