ID   PDUN_CITFR              Reviewed;          91 AA.
AC   P0DUV6;
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 vertex protein PduN {ECO:0000303|PubMed:20417607};
DE   AltName: Full=Bacterial microcompartment protein pentamer {ECO:0000305};
DE            Short=BMC-P {ECO:0000305};
DE   AltName: Full=Propanediol utilization protein PduN;
GN   Name=pduN {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, DOMAIN, 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: Probably forms vertices in the shell of the bacterial
CC       microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD)
CC       degradation. {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 BMC in its cytoplasm. Overexpression of this protein has
CC       no effect on the appearance of BMCs. {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: Homopentamer (By similarity). Interacts with shell protein
CC       PduA (PubMed:20417607). {ECO:0000250|UniProtKB:Q7NIT8,
CC       ECO:0000269|PubMed:20417607}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000269|PubMed:20417607}.
CC   -!- DOMAIN: The N-terminus is required for integration into BMCs; a C-
CC       terminal GFP fusion protein is targeted to BMCs whereas an N-terminal
CC       GFP fusion does not permit BMC formation.
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 CcmL/EutN family. {ECO:0000305}.
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DR   EMBL; AM498294; CAM57294.1; -; 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; cd01614; EutN_CcmL; 1.
DR   Gene3D; 2.40.50.220; -; 1.
DR   InterPro; IPR004992; EutN_CcmL.
DR   InterPro; IPR036677; EutN_CcmL_sf.
DR   PANTHER; PTHR36539; PTHR36539; 1.
DR   Pfam; PF03319; EutN_CcmL; 1.
DR   SUPFAM; SSF159133; SSF159133; 1.
DR   PROSITE; PS51932; BMV; 1.
PE   1: Evidence at protein level;
KW   Bacterial microcompartment.
FT   CHAIN           1..91
FT                   /note="Bacterial microcompartment shell vertex protein
FT                   PduN"
FT                   /id="PRO_0000454267"
FT   DOMAIN          1..87
FT                   /note="BMV"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01280"
SQ   SEQUENCE   91 AA;  9206 MW;  4A5343883765E02F CRC64;
     MHLARVTGVV VSTQKSPSLV GKKLLLVRRV SADGELPASP VSGDEVAVDS VGAGTGELVL
     LSSGSSARHV FSGPNEAIDL AIVGIVDTLS R