ID   PDUU_SALTI              Reviewed;         116 AA.
AC   P0A1D2; Q9XDM7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Bacterial microcompartment shell protein PduU {ECO:0000305};
DE   AltName: Full=Bacterial microcompartment protein homohexamer {ECO:0000305};
DE            Short=BMC-H {ECO:0000305};
DE   AltName: Full=Propanediol utilization protein PduU;
GN   Name=pduU; OrderedLocusNames=STY2260, t0819;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: A minor shell protein of the bacterial microcompartment (BMC)
CC       dedicated to 1,2-propanediol (1,2-PD) degradation. May selectively
CC       transport specific metabolites. Not absolutely required to make
CC       artificial BMCs (By similarity). Proteins such as this one with
CC       circularly permuted BMC domains may play a key role in conferring
CC       heterogeneity and flexibility in this BMC (Probable).
CC       {ECO:0000250|UniProtKB:P0A1D1, ECO:0000305}.
CC   -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC       {ECO:0000250|UniProtKB:P0A1D1}.
CC   -!- SUBUNIT: Homohexamer with a central pore lined by a beta-barrel.
CC       Hexamers pack into a loose array. Interacts with PduV, probably via the
CC       beta-barrel, which is predicted by modeling to be on the exterior of
CC       the BMC (By similarity). Interacts with shell protein PduA (By
CC       similarity). {ECO:0000250|UniProtKB:P0A1D1,
CC       ECO:0000250|UniProtKB:P0DUV8}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000250|UniProtKB:P0A1D1}.
CC   -!- INDUCTION: By propanediol. {ECO:0000250|UniProtKB:P0A1D1}.
CC   -!- DOMAIN: One side of the hexamer is concave which is lined by
CC       hydrophobic residues, the other side has a slightly protruding, 6-
CC       stranded beta-barrel. {ECO:0000250|UniProtKB:A0A0E2IV13}.
CC   -!- SIMILARITY: Belongs to the EutS/PduU family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01279, ECO:0000305}.
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DR   EMBL; AL513382; CAD02416.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68508.1; -; Genomic_DNA.
DR   RefSeq; NP_456604.1; NC_003198.1.
DR   RefSeq; WP_000441103.1; NZ_WSUR01000002.1.
DR   AlphaFoldDB; P0A1D2; -.
DR   SMR; P0A1D2; -.
DR   STRING; 220341.16503285; -.
DR   EnsemblBacteria; AAO68508; AAO68508; t0819.
DR   GeneID; 64335876; -.
DR   GeneID; 66587171; -.
DR   KEGG; stt:t0819; -.
DR   KEGG; sty:STY2260; -.
DR   PATRIC; fig|220341.7.peg.2279; -.
DR   eggNOG; COG4810; Bacteria.
DR   HOGENOM; CLU_143326_0_0_6; -.
DR   OMA; HIIPNPQ; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07046; BMC_PduU-EutS; 1.
DR   Gene3D; 3.30.70.1710; -; 1.
DR   InterPro; IPR044870; BMC_CP.
DR   InterPro; IPR000249; BMC_dom.
DR   InterPro; IPR037233; CcmK-like_sf.
DR   InterPro; IPR009307; EutS/PduU/CutR.
DR   PANTHER; PTHR40449; PTHR40449; 1.
DR   Pfam; PF00936; BMC; 1.
DR   PIRSF; PIRSF012296; EutS_PduU; 1.
DR   SMART; SM00877; BMC; 1.
DR   SUPFAM; SSF143414; SSF143414; 1.
DR   PROSITE; PS51931; BMC_CP; 1.
PE   3: Inferred from homology;
KW   Bacterial microcompartment; Transport.
FT   CHAIN           1..116
FT                   /note="Bacterial microcompartment shell protein PduU"
FT                   /id="PRO_0000201525"
FT   DOMAIN          9..108
FT                   /note="BMC circularly permuted"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
SQ   SEQUENCE   116 AA;  12476 MW;  39BEFE5E38F0D1F6 CRC64;
     MERQPTTDRM IQEYVPGKQV TLAHLIANPG KDLFKKLGLQ DAVSAIGILT ITPSEASIIA
     CDIATKSGAV EIGFLDRFTG AVVLTGDVSA VEYALKQVTR TLGEMMQFTT CSITRT