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}.
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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
//
