PDUN_SALTY
ID PDUN_SALTY Reviewed; 91 AA.
AC Q9XDN3; Q7BV77;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Bacterial microcompartment shell vertex protein PduN {ECO:0000303|PubMed:21239588};
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:10498708}; OrderedLocusNames=STM2049;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=10498708; DOI=10.1128/jb.181.19.5967-5975.1999;
RA Bobik T.A., Havemann G.D., Busch R.J., Williams D.S., Aldrich H.C.;
RT "The propanediol utilization (pdu) operon of Salmonella enterica serovar
RT typhimurium LT2 includes genes necessary for formation of polyhedral
RT organelles involved in coenzyme B(12)-dependent 1, 2-propanediol
RT degradation.";
RL J. Bacteriol. 181:5967-5975(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP BACTERIAL MICROCOMPARTMENT ABUNDANCE.
RC STRAIN=LT2;
RX PubMed=12923081; DOI=10.1128/jb.185.17.5086-5095.2003;
RA Havemann G.D., Bobik T.A.;
RT "Protein content of polyhedral organelles involved in coenzyme B12-
RT dependent degradation of 1,2-propanediol in Salmonella enterica serovar
RT Typhimurium LT2.";
RL J. Bacteriol. 185:5086-5095(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=21239588; DOI=10.1128/jb.01473-10;
RA Cheng S., Sinha S., Fan C., Liu Y., Bobik T.A.;
RT "Genetic analysis of the protein shell of the microcompartments involved in
RT coenzyme B12-dependent 1,2-propanediol degradation by Salmonella.";
RL J. Bacteriol. 193:1385-1392(2011).
RN [5]
RP BIOTECHNOLOGY (ARTIFICIAL BMCS).
RC STRAIN=LT2;
RX PubMed=24014666; DOI=10.1099/mic.0.069922-0;
RA Sargent F., Davidson F.A., Kelly C.L., Binny R., Christodoulides N.,
RA Gibson D., Johansson E., Kozyrska K., Lado L.L., MacCallum J., Montague R.,
RA Ortmann B., Owen R., Coulthurst S.J., Dupuy L., Prescott A.R., Palmer T.;
RT "A synthetic system for expression of components of a bacterial
RT microcompartment.";
RL Microbiology 159:2427-2436(2013).
RN [6]
RP SYSTEM-MODELING, AND FUNCTION.
RC STRAIN=LT2;
RX PubMed=28475631; DOI=10.1371/journal.pcbi.1005525;
RA Jakobson C.M., Tullman-Ercek D., Slininger M.F., Mangan N.M.;
RT "A systems-level model reveals that 1,2-Propanediol utilization
RT microcompartments enhance pathway flux through intermediate
RT sequestration.";
RL PLoS Comput. Biol. 13:e1005525-e1005525(2017).
CC -!- FUNCTION: Probably forms vertices in the shell of the bacterial
CC microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD)
CC degradation. Required for structural integrity of BMCs and to mitigate
CC propionaldehyde toxicity. {ECO:0000269|PubMed:21239588}.
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:28475631}.
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000305|PubMed:10498708}.
CC -!- SUBUNIT: Homopentamer (By similarity). Interacts with shell protein
CC PduA (By similarity). {ECO:0000250|UniProtKB:P0DUV6,
CC ECO:0000250|UniProtKB:Q7NIT8}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:21239588}.
CC -!- INDUCTION: BMC production is induced by growth on 1,2-PD vitamin B12
CC medium. {ECO:0000269|PubMed:10498708}.
CC -!- DISRUPTION PHENOTYPE: Forms BMCs with a variety of morphologies,
CC including elongated, enlarged, and aggregated MCPs and some with
CC rounded cross-sections. Grows in an interrupted manner on 1,2-PD and
CC vitamin B12; grows for a while then stops, then restarts as if a toxic
CC compound was accumulating and then decreases.
CC {ECO:0000269|PubMed:21239588}.
CC -!- BIOTECHNOLOGY: Artificial BMCs can be made in E.coli by expressing
CC pduA-pduB/B'-pduT-pduU-pduN-pduJ-pduK (in this order). Enzymes can be
CC targeted to the BMC, and appear to be encapsulated within it.
CC {ECO:0000269|PubMed:24014666}.
CC -!- MISCELLANEOUS: Bacterial microcompartments (BMC) 100-200 nm in cross
CC section are formed during aerobic growth on minimal 1,2-PD-B12 or
CC anaerobic growth on 1,2-PD-tetrathionate medium, but not during aerobic
CC growth on glucose, anerobic growth on glucose or pyruvate-tetrathionate
CC (PubMed:10498708). BMCs can constitute up to 10% of total cell protein
CC (PubMed:12923081). {ECO:0000269|PubMed:10498708,
CC ECO:0000269|PubMed:12923081}.
CC -!- SIMILARITY: Belongs to the CcmL/EutN family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF026270; AAD39013.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20953.1; -; Genomic_DNA.
DR RefSeq; NP_460994.1; NC_003197.2.
DR RefSeq; WP_000549824.1; NC_003197.2.
DR AlphaFoldDB; Q9XDN3; -.
DR SMR; Q9XDN3; -.
DR STRING; 99287.STM2049; -.
DR PaxDb; Q9XDN3; -.
DR EnsemblBacteria; AAL20953; AAL20953; STM2049.
DR GeneID; 1253570; -.
DR KEGG; stm:STM2049; -.
DR PATRIC; fig|99287.12.peg.2171; -.
DR HOGENOM; CLU_148498_3_0_6; -.
DR OMA; ICTDEVE; -.
DR PhylomeDB; Q9XDN3; -.
DR BioCyc; SENT99287:STM2049-MON; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031472; C:propanediol degradation polyhedral organelle; IDA:UniProtKB.
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; Reference proteome.
FT CHAIN 1..91
FT /note="Bacterial microcompartment shell vertex protein
FT PduN"
FT /id="PRO_0000454268"
FT DOMAIN 1..87
FT /note="BMV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01280"
SQ SEQUENCE 91 AA; 9094 MW; FC58E311D3E2CEBA CRC64;
MHLARVTGAV VSTQKSPSLI GKKLLLVRRV SADGELPASP TSGDEVAVDS VGAGVGELVL
LSGGSSARHV FSGPNEAIDL AVVGIVDTLS C
