PDUM_SALTY
ID PDUM_SALTY Reviewed; 163 AA.
AC Q9XDN4; Q7BV78;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Bacterial microcompartment assembly protein PduM {ECO:0000303|PubMed:22343294};
DE AltName: Full=Propanediol utilization protein PduM {ECO:0000303|PubMed:10498708};
GN Name=pduM {ECO:0000303|PubMed:10498708}; OrderedLocusNames=STM2048;
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 PROTEIN SEQUENCE OF 9-16; 20-48 AND 72-82, FUNCTION, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=22343294; DOI=10.1128/jb.06529-11;
RA Sinha S., Cheng S., Fan C., Bobik T.A.;
RT "The PduM protein is a structural component of the microcompartments
RT involved in coenzyme B(12)-dependent 1,2-propanediol degradation by
RT Salmonella enterica.";
RL J. Bacteriol. 194:1912-1918(2012).
RN [4]
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 [5]
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: Plays an essential role in assembly and/or stability of the
CC bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD)
CC degradation. Overexpression impairs BMC formation.
CC {ECO:0000269|PubMed:22343294}.
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: Interacts with shell protein PduK.
CC {ECO:0000250|UniProtKB:B1VB72}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:22343294}.
CC -!- INDUCTION: BMC production is induced by growth on 1,2-PD vitamin B12
CC medium. {ECO:0000269|PubMed:10498708}.
CC -!- DISRUPTION PHENOTYPE: Impaired for BMC assembly, with a disrupted,
CC unstable BMC shell. {ECO:0000269|PubMed:22343294}.
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 PduM family. {ECO:0000305}.
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DR EMBL; AF026270; AAD39012.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20952.1; -; Genomic_DNA.
DR RefSeq; NP_460993.1; NC_003197.2.
DR RefSeq; WP_001012956.1; NC_003197.2.
DR AlphaFoldDB; Q9XDN4; -.
DR STRING; 99287.STM2048; -.
DR PaxDb; Q9XDN4; -.
DR EnsemblBacteria; AAL20952; AAL20952; STM2048.
DR GeneID; 1253569; -.
DR KEGG; stm:STM2048; -.
DR PATRIC; fig|99287.12.peg.2170; -.
DR HOGENOM; CLU_137852_0_0_6; -.
DR OMA; MLMQRIV; -.
DR BioCyc; SENT99287:STM2048-MON; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031472; C:propanediol degradation polyhedral organelle; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:1902117; P:positive regulation of organelle assembly; IMP:UniProtKB.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR030992; PduM.
DR Pfam; PF15953; PDU_like; 1.
DR TIGRFAMs; TIGR04493; microcomp_PduM; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Direct protein sequencing; Reference proteome.
FT CHAIN 1..163
FT /note="Bacterial microcompartment assembly protein PduM"
FT /id="PRO_0000454266"
SQ SEQUENCE 163 AA; 17914 MW; FB0B71A042F92B65 CRC64;
MNGETLQRIV EEIVSRLHRR AQSTATLSVT QLRDADCPAL FCQHASLRIL LIDLPLLGQL
ADAETGDAAA RKIHDALAFG IRVQLSLHSQ LLPVIPVKKL ARLPLVFTDE HGLPLVLHAG
SVLSYRDVAL LSRGRVVVHR KCIVTAMARD AANARNIQLI KQE
