ID PDUA_SALTY Reviewed; 94 AA. AC P0A1C7; P37448; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 90. DE RecName: Full=Bacterial microcompartment shell protein PduA {ECO:0000303|PubMed:11844753}; DE AltName: Full=Bacterial microcompartment protein homohexamer {ECO:0000305}; DE Short=BMC-H {ECO:0000303|PubMed:33227310}; DE AltName: Full=Propanediol utilization protein PduA; GN Name=pduA {ECO:0000303|PubMed:8071226}; OrderedLocusNames=STM2038; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RX PubMed=8071226; DOI=10.1128/jb.176.17.5474-5482.1994; RA Chen P., Anderson D.I., Roth J.R.; RT "The control region of the pdu/cob regulon in Salmonella typhimurium."; RL J. Bacteriol. 176:5474-5482(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RX PubMed=9352910; DOI=10.1128/jb.179.21.6633-6639.1997; RA Bobik T.A., Xu Y., Jeter R.M., Otto K.E., Roth J.R.; RT "Propanediol utilization genes (pdu) of Salmonella typhimurium: three genes RT for the propanediol dehydratase."; RL J. Bacteriol. 179:6633-6639(1997). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, SEQUENCE REVISION TO RP C-TERMINUS, 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 [5] RP PROTEIN SEQUENCE OF 1-7, FUNCTION, AND SUBCELLULAR LOCATION. 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 [6] RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RC STRAIN=LT2; RX PubMed=11844753; DOI=10.1128/jb.184.5.1253-1261.2002; RA Havemann G.D., Sampson E.M., Bobik T.A.; RT "PduA is a shell protein of polyhedral organelles involved in coenzyme RT B(12)-dependent degradation of 1,2-propanediol in Salmonella enterica RT serovar typhimurium LT2."; RL J. Bacteriol. 184:1253-1261(2002). RN [7] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=LT2; RX PubMed=18296526; DOI=10.1128/jb.01925-07; RA Sampson E.M., Bobik T.A.; RT "Microcompartments for B12-dependent 1,2-propanediol degradation provide RT protection from DNA and cellular damage by a reactive metabolic RT intermediate."; RL J. Bacteriol. 190:2966-2971(2008). RN [8] RP FUNCTION, 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 [9] RP FUNCTION, INTERACTION WITH PDUP, DOMAIN, AND MUTAGENESIS OF 81-HIS--SER-93; RP HIS-81; VAL-84 AND LEU-88. RC STRAIN=LT2; RX PubMed=22927404; DOI=10.1073/pnas.1207516109; RA Fan C., Cheng S., Sinha S., Bobik T.A.; RT "Interactions between the termini of lumen enzymes and shell proteins RT mediate enzyme encapsulation into bacterial microcompartments."; RL Proc. Natl. Acad. Sci. U.S.A. 109:14995-15000(2012). RN [10] 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 [11] RP MODELING OF BMCS, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=25646976; DOI=10.1371/journal.pcbi.1004067; RA Jorda J., Liu Y., Bobik T.A., Yeates T.O.; RT "Exploring bacterial organelle interactomes: a model of the protein-protein RT interaction network in the Pdu microcompartment."; RL PLoS Comput. Biol. 11:e1004067-e1004067(2015). RN [12] RP FUNCTION, AND INDUCTION. RC STRAIN=LT2; RX PubMed=26283792; DOI=10.1074/jbc.m115.651919; RA Jakobson C.M., Kim E.Y., Slininger M.F., Chien A., Tullman-Ercek D.; RT "Localization of proteins to the 1,2-propanediol utilization RT microcompartment by non-native signal sequences is mediated by a common RT hydrophobic motif."; RL J. Biol. Chem. 290:24519-24533(2015). RN [13] RP SUBCELLULAR LOCATION. RC STRAIN=LT2; RX PubMed=27063436; DOI=10.1038/srep24359; RA Held M., Kolb A., Perdue S., Hsu S.Y., Bloch S.E., Quin M.B., RA Schmidt-Dannert C.; RT "Engineering formation of multiple recombinant Eut protein nanocompartments RT in E. coli."; RL Sci. Rep. 6:24359-24359(2016). RN [14] RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-40. RC STRAIN=LT2; RX PubMed=27561553; DOI=10.1111/mmi.13423; RA Chowdhury C., Chun S., Sawaya M.R., Yeates T.O., Bobik T.A.; RT "The function of the PduJ microcompartment shell protein is determined by RT the genomic position of its encoding gene."; RL Mol. Microbiol. 101:770-783(2016). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF RP LYS-26 AND LYS-37. RC STRAIN=LT2; RX PubMed=28585808; DOI=10.1021/acssynbio.7b00042; RA Slininger Lee M.F., Jakobson C.M., Tullman-Ercek D.; RT "Evidence for Improved Encapsulated Pathway Behavior in a Bacterial RT Microcompartment through Shell Protein Engineering."; RL ACS Synth. Biol. 6:1880-1891(2017). RN [16] RP FUNCTION IN METABOLITE DIFFUSION. RC STRAIN=LT2; RX PubMed=28829618; DOI=10.1021/acs.jpcb.7b07232; RA Park J., Chun S., Bobik T.A., Houk K.N., Yeates T.O.; RT "Molecular Dynamics Simulations of Selective Metabolite Transport across RT the Propanediol Bacterial Microcompartment Shell."; RL J. Phys. Chem. B 121:8149-8154(2017). RN [17] 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). RN [18] RP BIOTECHNOLOGY (FORMING PROTEIN SHELLS), AND MUTAGENESIS OF LYS-26. RC STRAIN=LT2; RX PubMed=31845931; DOI=10.1039/c9tb02224d; RA Bari N.K., Kumar G., Hazra J.P., Kaur S., Sinha S.; RT "Functional protein shells fabricated from the self-assembling protein RT sheets of prokaryotic organelles."; RL J. Mater. Chem. B 8:523-533(2020). RN [19] RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-26. RC STRAIN=LT2; RX PubMed=33227310; DOI=10.1016/j.jmb.2020.11.020; RA Kennedy N.W., Ikonomova S.P., Slininger Lee M., Raeder H.W., RA Tullman-Ercek D.; RT "Self-assembling Shell Proteins PduA and PduJ have Essential and Redundant RT Roles in Bacterial Microcompartment Assembly."; RL J. Mol. Biol. 433:166721-166721(2021). RN [20] {ECO:0007744|PDB:3NGK} RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 2-94, FUNCTION, AND SUBUNIT. RC STRAIN=LT2; RX PubMed=20870711; DOI=10.1074/jbc.m110.160580; RA Crowley C.S., Cascio D., Sawaya M.R., Kopstein J.S., Bobik T.A., RA Yeates T.O.; RT "Structural insight into the mechanisms of transport across the Salmonella RT enterica Pdu microcompartment shell."; RL J. Biol. Chem. 285:37838-37846(2010). RN [21] {ECO:0007744|PDB:4PPD} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-94, FUNCTION, SUBUNIT, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-26; ASN-29; LYS-37; LYS-55 AND RP ARG-79. RC STRAIN=LT2; RX PubMed=24747050; DOI=10.1016/j.jmb.2014.04.012; RA Sinha S., Cheng S., Sung Y.W., McNamara D.E., Sawaya M.R., Yeates T.O., RA Bobik T.A.; RT "Alanine scanning mutagenesis identifies an asparagine-arginine-lysine RT triad essential to assembly of the shell of the Pdu microcompartment."; RL J. Mol. Biol. 426:2328-2345(2014). RN [22] {ECO:0007744|PDB:4QIE} RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2-94, AND SUBUNIT. RA Pang A.H., Sawaya M.R., Bobik T.A., Yeates T.O.; RT "Crystal Structure of PduA with edge mutation K26D."; RL Submitted (MAY-2014) to the PDB data bank. RN [23] {ECO:0007744|PDB:4QIF, ECO:0007744|PDB:4QIG, ECO:0007744|PDB:4RBT, ECO:0007744|PDB:4RBU, ECO:0007744|PDB:4RBV} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-94, FUNCTION, SUBUNIT, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-40. RC STRAIN=LT2; RX PubMed=25713376; DOI=10.1073/pnas.1423672112; RA Chowdhury C., Chun S., Pang A., Sawaya M.R., Sinha S., Yeates T.O., RA Bobik T.A.; RT "Selective molecular transport through the protein shell of a bacterial RT microcompartment organelle."; RL Proc. Natl. Acad. Sci. U.S.A. 112:2990-2995(2015). CC -!- FUNCTION: One of the major shell proteins of the bacterial CC microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) CC degradation (PubMed:11844753, PubMed:21239588) (Probable). At least one CC of PduA or PduJ is required for BMC assembly; it must be encoded as the CC first gene in the pdu operon (PubMed:33227310, PubMed:27561553). Not CC required for structural integrity of BMCs, it is required to mitigate CC propionaldehyde toxicity (PubMed:21239588). Controls diffusion of 1,2- CC PD into and propionaldehyde out of the BMC shell; residue 40 is CC particularly important for pore permeability (PubMed:28585808, CC PubMed:25713376, PubMed:27561553) (Probable). Overexpression of this CC protein leads to aberrant filaments that extend the length of the cell, CC cross the cleavage furrow and impair division. The filaments form CC nanotubes with a hollow center (PubMed:11844753, PubMed:33227310). The CC isolated BMC shell component protein ratio for J:A:B':B:K:T:U is CC approximately 15:10:7:6:1:1:2 (PubMed:12923081). Edge residues CC (particularly Lys-26) are important for function and assembly of the CC BMC, and influence array formation by hexamers (PubMed:24747050). CC Interaction with PduA allows encapsulation of at least PduP in BMCs CC (PubMed:22927404). Probably also targets PduD to the BMC (Probable). CC PduA is probably the hub for binding multiple enzymes to the interior CC of the BMC; modeling suggests PduC, PduD, PduE, PduG, PduL and PduP are CC targeted to PduA (Probable). {ECO:0000269|PubMed:11844753, CC ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:21239588, CC ECO:0000269|PubMed:22927404, ECO:0000269|PubMed:24747050, CC ECO:0000269|PubMed:25713376, ECO:0000269|PubMed:27561553, CC ECO:0000269|PubMed:28585808, ECO:0000269|PubMed:33227310, CC ECO:0000305|PubMed:20870711, ECO:0000305|PubMed:24747050, CC ECO:0000305|PubMed:25646976, ECO:0000305|PubMed:26283792, CC ECO:0000305|PubMed:28829618}. 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:0000269|PubMed:18296526, ECO:0000269|PubMed:25713376, CC ECO:0000305|PubMed:28475631}. CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation. CC {ECO:0000305|PubMed:10498708}. CC -!- SUBUNIT: Homohexamer with a central pore of about 5.6 Angstroms in CC diameter. The hexamers pack against each other in arrays CC (PubMed:20870711, PubMed:24747050, Ref.22, PubMed:25713376). Interacts CC with the N-terminus of PduP which targets PduP to the BMC CC (PubMed:22927404). Modeling suggests PduC, PduD, PduE, PduL and PduP CC interact with a cleft formed by the C-terminal segments of 2 adjacent CC PduA subunits (on the BMC luminal side) in the hexamer (Probable). CC {ECO:0000269|PubMed:20870711, ECO:0000269|PubMed:22927404, CC ECO:0000269|PubMed:24747050, ECO:0000269|PubMed:25713376, CC ECO:0000269|Ref.22, ECO:0000305|PubMed:25646976}. CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment CC {ECO:0000269|PubMed:11844753, ECO:0000269|PubMed:12923081, CC ECO:0000269|PubMed:24747050, ECO:0000269|PubMed:25713376, CC ECO:0000269|PubMed:27063436, ECO:0000269|PubMed:28585808}. Note=The C- CC terminus probably faces the interior of the BMC (Probable). Modeling CC suggests the concave face (with both termini) is in the interior of the CC BMC (Probable). {ECO:0000305|PubMed:22927404, CC ECO:0000305|PubMed:25646976}. CC -!- INDUCTION: The first gene in the pdu operon. BMC production is induced CC by growth on 1,2-PD vitamin B12 medium (PubMed:10498708, CC PubMed:26283792). No change when grown in the presence of 1,2-PD, CC ethanolamine and vitamin B12, suggesting it is possible for both the CC eut and pdu operons to be expressed at the same time (PubMed:26283792). CC {ECO:0000269|PubMed:10498708, ECO:0000269|PubMed:26283792}. CC -!- DOMAIN: The C-terminal 14 residues mediate binding to the N-terminus of CC PduP, which encapsulates PduP into BMCs. {ECO:0000269|PubMed:22927404}. CC -!- DISRUPTION PHENOTYPE: Cells do not make BMCs, diol dehydratase is found CC in diffuse aggregates near the cell pole; it was later found this a CC double pduA-pduBB' deletion (PubMed:11844753). A single deletion forms CC larger than normal BMCs; it is not fully complemented by protein CC produced from a plasmid (PubMed:21239588, PubMed:27561553). Grows in an CC interrupted manner on 1,2-PD and vitamin B12; grows for a while then CC stops, then restarts as toxic propionaldehyde accumulates and then CC decreases (PubMed:11844753, PubMed:28585808, PubMed:21239588, CC PubMed:18296526, PubMed:33227310). Increased DNA mutagenesis, showing CC propionaldehyde is a mutagen (PubMed:18296526). Makes slightly larger CC BMCs; this phenotype can be rescued by PduA, but PduJ encoded on a CC plasmid cannot rescue a PduA deletion. When pduJ is cloned in the CC chromosomal position of pduA it substantially rescues the pduA deletion CC (PubMed:27561553, PubMed:33227310). Single pduA deletion makes BMCs but CC a double pduA-pduJ deletion does not (PubMed:33227310). CC {ECO:0000269|PubMed:11844753, ECO:0000269|PubMed:18296526, CC ECO:0000269|PubMed:21239588, ECO:0000269|PubMed:27561553, CC ECO:0000269|PubMed:28585808, ECO:0000269|PubMed:33227310}. 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 -!- BIOTECHNOLOGY: Upon overexpression and mixing of purified sheets with CC 2-ethyl-1-hexanol, will form closed shells. Enzymes (tested with CC endogenous BMC enzyme DDH and the peroxidase activity of cytC) can be CC encapsulated in the shells; the enzyme is active in the shells. The CC shells are permeable to a variety of compounds, showing they could be CC used to make protein based synthetic bioreactors. CC {ECO:0000269|PubMed:31845931}. 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 bacterial microcompartments protein family. CC {ECO:0000255|PROSITE-ProRule:PRU01278}. 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; AAB84107.2; -; Genomic_DNA. DR EMBL; AE006468; AAL20942.1; -; Genomic_DNA. DR RefSeq; NP_460983.1; NC_003197.2. DR RefSeq; WP_001183618.1; NC_003197.2. DR PDB; 3NGK; X-ray; 2.26 A; A=2-94. DR PDB; 4PPD; X-ray; 2.40 A; A/B/C/D/E/F/G=2-94. DR PDB; 4QIE; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I=2-94. DR PDB; 4QIF; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I=2-94. DR PDB; 4QIG; X-ray; 3.30 A; A/B/C/D/E/F/G=2-94. DR PDB; 4RBT; X-ray; 2.30 A; A/B/C=2-94. DR PDB; 4RBU; X-ray; 2.79 A; A/B/C/D/E/F/G/H/I=2-94. DR PDB; 4RBV; X-ray; 3.10 A; A/B/C/D/E/F/G=2-94. DR PDBsum; 3NGK; -. DR PDBsum; 4PPD; -. DR PDBsum; 4QIE; -. DR PDBsum; 4QIF; -. DR PDBsum; 4QIG; -. DR PDBsum; 4RBT; -. DR PDBsum; 4RBU; -. DR PDBsum; 4RBV; -. DR AlphaFoldDB; P0A1C7; -. DR SMR; P0A1C7; -. DR STRING; 99287.STM2038; -. DR TCDB; 1.S.1.1.1; the bacterial microcompartment shell/pore-forming protein-1 (bmc-sp1) family. DR PaxDb; 99287-STM2038; -. DR GeneID; 1253559; -. DR GeneID; 77226968; -. DR KEGG; stm:STM2038; -. DR PATRIC; fig|99287.12.peg.2160; -. DR HOGENOM; CLU_064903_5_3_6; -. DR OMA; HSEVEMI; -. DR PhylomeDB; P0A1C7; -. DR BioCyc; SENT99287:STM2038-MONOMER; -. 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; cd07045; BMC_CcmK_like; 1. DR Gene3D; 3.30.70.1710; -; 1. DR InterPro; IPR020808; Bact_microcomp_CS. DR InterPro; IPR000249; BMC_dom. DR InterPro; IPR037233; CcmK-like_sf. DR InterPro; IPR044872; CcmK/CsoS1_BMC. DR PANTHER; PTHR33941:SF11; BACTERIAL MICROCOMPARTMENT SHELL PROTEIN PDUJ; 1. DR PANTHER; PTHR33941; PROPANEDIOL UTILIZATION PROTEIN PDUA; 1. DR Pfam; PF00936; BMC; 1. DR SMART; SM00877; BMC; 1. DR SUPFAM; SSF143414; CcmK-like; 1. DR PROSITE; PS01139; BMC_1; 1. DR PROSITE; PS51930; BMC_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Bacterial microcompartment; Direct protein sequencing; KW Reference proteome; Transport. FT CHAIN 1..94 FT /note="Bacterial microcompartment shell protein PduA" FT /id="PRO_0000201511" FT DOMAIN 5..89 FT /note="BMC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278" FT MUTAGEN 26 FT /note="K->A: No BMCs are made, forms hexamers which do not FT form arrays, dominant to wild-type protein. Little to no FT growth on 1,2-PD, cells elongate and are joined by FT filaments, BMC proteins aggregate near poles. No longer FT forms filaments upon overexpression, does not restore BMC FT formation to a double pduA-pduJ deletion. Does not form FT closed shells." FT /evidence="ECO:0000269|PubMed:24747050, FT ECO:0000269|PubMed:28585808, ECO:0000269|PubMed:31845931, FT ECO:0000269|PubMed:33227310" FT MUTAGEN 29 FT /note="N->A: Subject to propionaldehyde toxicity, makes FT about 75% BMCs, shells are wrinkled and leaky." FT /evidence="ECO:0000269|PubMed:24747050" FT MUTAGEN 37 FT /note="K->A: Slow growth at limiting vitamin B12, wild-type FT at saturating conditions." FT /evidence="ECO:0000269|PubMed:24747050" FT MUTAGEN 37 FT /note="K->Q: Improved growth on 1,2-PD, makes slightly FT larger BMCs, alters accumulation of PD metabolites." FT /evidence="ECO:0000269|PubMed:28585808" FT MUTAGEN 40 FT /note="S->A: No change in shell permeability to PD, FT excretes more propionaldehyde, wild-type growth on 1,2-PD." FT /evidence="ECO:0000269|PubMed:25713376" FT MUTAGEN 40 FT /note="S->C: Crystallized, central pore can be open or FT occluded, less permeable to substrate, cells grow slowly on FT 1,2-PD." FT /evidence="ECO:0000269|PubMed:25713376" FT MUTAGEN 40 FT /note="S->GSG: Crystallized, central pore is occluded, less FT permeable to PD, 62% DDH activity, cells grow slowly on FT 1,2-PD." FT /evidence="ECO:0000269|PubMed:25713376" FT MUTAGEN 40 FT /note="S->H: Crystallized, central pore is less symmetric, FT no change in shell permeability, increased permeability to FT glycerol, wild-type growth on 1,2-PD." FT /evidence="ECO:0000269|PubMed:25713376" FT MUTAGEN 40 FT /note="S->L: Crystallized, central pore is more hydrophobic FT but same size, less permeable to PD, 50% DDH activity, FT cells grow slowly on 1,2-PD." FT /evidence="ECO:0000269|PubMed:25713376, FT ECO:0000269|PubMed:27561553" FT MUTAGEN 40 FT /note="S->M: No change in shell permeability, wild-type FT growth on 1,2-PD." FT /evidence="ECO:0000269|PubMed:25713376" FT MUTAGEN 40 FT /note="S->Q: Crystallized, central pore is occluded, less FT permeable to substrate, 75% DDH activity, cells grow slowly FT on 1,2-PD." FT /evidence="ECO:0000269|PubMed:25713376" FT MUTAGEN 40 FT /note="S->T: No change in shell permeability, wild-type FT growth on 1,2-PD." FT /evidence="ECO:0000269|PubMed:25713376" FT MUTAGEN 55 FT /note="K->A: Slow growth at limiting vitamin B12, wild-type FT at saturating conditions." FT /evidence="ECO:0000269|PubMed:24747050" FT MUTAGEN 79 FT /note="R->A: Subject to propionaldehyde toxicity, makes FT about 70% BMCs, protein shells appear wild-type but leak." FT /evidence="ECO:0000269|PubMed:24747050" FT MUTAGEN 81..93 FT /note="Missing: No longer interacts with PduP." FT /evidence="ECO:0000269|PubMed:22927404" FT MUTAGEN 81 FT /note="H->A: Decreased amounts of PduP in purified BMCs." FT /evidence="ECO:0000269|PubMed:22927404" FT MUTAGEN 84 FT /note="V->A: Decreased amounts of PduP in purified BMCs." FT /evidence="ECO:0000269|PubMed:22927404" FT MUTAGEN 88 FT /note="L->A: Decreased amounts of PduP in purified BMCs." FT /evidence="ECO:0000269|PubMed:22927404" FT STRAND 4..13 FT /evidence="ECO:0007829|PDB:4QIF" FT HELIX 14..24 FT /evidence="ECO:0007829|PDB:4QIF" FT STRAND 30..39 FT /evidence="ECO:0007829|PDB:4QIF" FT STRAND 42..50 FT /evidence="ECO:0007829|PDB:4QIF" FT HELIX 51..66 FT /evidence="ECO:0007829|PDB:4QIF" FT STRAND 69..78 FT /evidence="ECO:0007829|PDB:4QIF" FT TURN 82..87 FT /evidence="ECO:0007829|PDB:4QIF" SQ SEQUENCE 94 AA; 9592 MW; 5EDC7C793F19DE1E CRC64; MQQEALGMVE TKGLTAAIEA ADAMVKSANV MLVGYEKIGS GLVTVIVRGD VGAVKAATDA GAAAARNVGE VKAVHVIPRP HTDVEKILPK GISQ //