PDUB_LIMRD
ID PDUB_LIMRD Reviewed; 238 AA.
AC A5VMB3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Bacterial microcompartment shell protein PduB;
DE AltName: Full=Bacterial microcompartment protein homotrimer {ECO:0000305};
DE Short=BMC-T {ECO:0000305};
DE AltName: Full=Propanediol utilization protein PduB;
GN Name=pduB {ECO:0000303|PubMed:23151629}; OrderedLocusNames=Lreu_1748;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
RN [2] {ECO:0007744|PDB:4FAY}
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS), GLYCEROL-BINDING, SUBUNIT, AND
RP DISULFIDE BONDS.
RC STRAIN=DSM 20016;
RX PubMed=23151629; DOI=10.1107/s0907444912039315;
RA Pang A., Liang M., Prentice M.B., Pickersgill R.W.;
RT "Substrate channels revealed in the trimeric Lactobacillus reuteri
RT bacterial microcompartment shell protein PduB.";
RL Acta Crystallogr. D 68:1642-1652(2012).
CC -!- FUNCTION: One of the major shell proteins of the bacterial
CC microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD)
CC degradation (By similarity). Probably involved in a propanediol
CC fermentation/reuterin formation pathway (Probable).
CC {ECO:0000250|UniProtKB:P37449, ECO:0000305|PubMed:21379339}.
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000305|PubMed:21379339}.
CC -!- SUBUNIT: Homotrimerizes to form a pseudohexamer with a central pore 7.5
CC Angstroms wide and 22 Angstroms long; the pore channel in the crystal
CC binds up to 4 glycerol molecules. A disulfide bond forms in the pore,
CC it is not clear if this is an artifact. The trimers pack into an array.
CC {ECO:0000269|PubMed:23151629}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000250|UniProtKB:P37449}.
CC -!- DOMAIN: Has 2 BMC domains which can evolve independently of each other.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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DR EMBL; CP000705; ABQ83987.1; -; Genomic_DNA.
DR RefSeq; WP_003669200.1; NZ_AZDD01000003.1.
DR PDB; 4FAY; X-ray; 1.56 A; A/B/C=1-238.
DR PDBsum; 4FAY; -.
DR SMR; A5VMB3; -.
DR STRING; 557436.Lreu_1748; -.
DR PRIDE; A5VMB3; -.
DR EnsemblBacteria; ABQ83987; ABQ83987; Lreu_1748.
DR GeneID; 66471924; -.
DR KEGG; lre:Lreu_1748; -.
DR PATRIC; fig|557436.17.peg.1055; -.
DR eggNOG; COG4816; Bacteria.
DR HOGENOM; CLU_076302_0_0_9; -.
DR OMA; YANDAGH; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001991; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.1710; -; 2.
DR InterPro; IPR044870; BMC_CP.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR009193; EutL_PduB.
DR InterPro; IPR030984; PduB.
DR Pfam; PF00936; BMC; 2.
DR PIRSF; PIRSF012290; EutL_PduB; 1.
DR SMART; SM00877; BMC; 2.
DR SUPFAM; SSF143414; SSF143414; 2.
DR TIGRFAMs; TIGR04501; microcomp_PduB; 1.
DR PROSITE; PS51931; BMC_CP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Disulfide bond;
KW Reference proteome.
FT CHAIN 1..238
FT /note="Bacterial microcompartment shell protein PduB"
FT /id="PRO_0000454248"
FT DOMAIN 14..125
FT /note="BMC circularly permuted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT DOMAIN 126..225
FT /note="BMC circularly permuted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT DISULFID 158..197
FT /evidence="ECO:0000305|PubMed:23151629,
FT ECO:0007744|PDB:4FAY"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:4FAY"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:4FAY"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:4FAY"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:4FAY"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:4FAY"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:4FAY"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:4FAY"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:4FAY"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:4FAY"
FT HELIX 204..223
FT /evidence="ECO:0007829|PDB:4FAY"
SQ SEQUENCE 238 AA; 24945 MW; 5A7ECF114249168C CRC64;
MNDFLNSTST VPEFVGASEI GDTIGMVIPR VDQQLLDKLH VTKQYKTLGI LSDRTGAGPQ
IMAMDEGIKA TNMECIDVEW PRDTKGGGGH GCLIIIGGDD PADARQAIRV ALDNLHRTFG
DVYNAKAGHL ELQFTARAAG AAHLGLGAVE GKAFGLICGC PSGIGVVMGD KALKTAGVEP
LNFTSPSHGT SFSNEGCLTI TGDSGAVRQA VMAGREVGLK LLSQFGEEPV NDFPSYIK
