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 24-JAN-2024, entry version 86. 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; Pseudomonadota; 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}. 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; 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.gene:17586171; -. DR GeneID; 69794646; -. 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 OrthoDB; 5457140at2; -. 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:SF2; BACTERIAL MICROCOMPARTMENT SHELL PROTEIN EUTS; 1. DR PANTHER; PTHR40449; ETHANOLAMINE UTILIZATION PROTEIN EUTS; 1. DR Pfam; PF00936; BMC; 1. DR PIRSF; PIRSF012296; EutS_PduU; 1. DR SMART; SM00877; BMC; 1. DR SUPFAM; SSF143414; CcmK-like; 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 //