EUTM_SALTY
ID EUTM_SALTY Reviewed; 96 AA.
AC P41791;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Bacterial microcompartment shell protein EutM;
DE AltName: Full=Bacterial microcompartment protein homohexamer {ECO:0000305};
DE Short=BMC-H {ECO:0000305};
DE AltName: Full=Ethanolamine utilization protein EutM;
GN Name=eutM {ECO:0000303|PubMed:10464203};
GN Synonyms=cchA {ECO:0000303|PubMed:7868611}; OrderedLocusNames=STM2465;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POSSIBLE FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=7868611; DOI=10.1128/jb.177.5.1357-1366.1995;
RA Stojiljkovic I., Baeumler A.J., Heffron F.;
RT "Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence,
RT protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG
RT eutH gene cluster.";
RL J. Bacteriol. 177:1357-1366(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=10464203; DOI=10.1128/jb.181.17.5317-5329.1999;
RA Kofoid E.C., Rappleye C.A., Stojiljkovic I., Roth J.R.;
RT "The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes
RT five homologues of carboxysome shell proteins.";
RL J. Bacteriol. 181:5317-5329(1999).
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 FUNCTION, PATHWAY, OPERON, AND INDUCTION BY ETHANOLAMINE AND COBALAMIN.
RC STRAIN=LT2;
RX PubMed=3045078; DOI=10.1128/jb.170.9.3855-3863.1988;
RA Roof D.M., Roth J.R.;
RT "Ethanolamine utilization in Salmonella typhimurium.";
RL J. Bacteriol. 170:3855-3863(1988).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16291677; DOI=10.1128/jb.187.23.8039-8046.2005;
RA Brinsmade S.R., Paldon T., Escalante-Semerena J.C.;
RT "Minimal functions and physiological conditions required for growth of
RT salmonella enterica on ethanolamine in the absence of the metabolosome.";
RL J. Bacteriol. 187:8039-8046(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16585748; DOI=10.1128/jb.188.8.2865-2874.2006;
RA Penrod J.T., Roth J.R.;
RT "Conserving a volatile metabolite: a role for carboxysome-like organelles
RT in Salmonella enterica.";
RL J. Bacteriol. 188:2865-2874(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=LT2;
RX PubMed=22428024; DOI=10.1371/journal.pone.0033342;
RA Choudhary S., Quin M.B., Sanders M.A., Johnson E.T., Schmidt-Dannert C.;
RT "Engineered protein nano-compartments for targeted enzyme localization.";
RL PLoS ONE 7:e33342-e33342(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=23585538; DOI=10.1128/jb.02179-12;
RA Huseby D.L., Roth J.R.;
RT "Evidence that a metabolic microcompartment contains and recycles private
RT cofactor pools.";
RL J. Bacteriol. 195:2864-2879(2013).
RN [9]
RP FUNCTION, INTERACTION WITH EUTQ, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, BIOTECHNOLOGY, AND MUTAGENESIS OF VAL-49;
RP 50-ALA--ALA-60; LYS-53; ALA-54; ASP-57; ALA-58; ALA-61; GLN-64 AND ARG-65.
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 [10]
RP FUNCTION, BIOTECHNOLOGY, AND MUTAGENESIS OF LYS-24.
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 [11]
RP BIOTECHNOLOGY.
RC STRAIN=LT2;
RX DOI=10.1021/acscatal.8b00986;
RA Zhang G., Quin M.B., Schmidt-Dannert C.;
RT "Self-Assembling Protein Scaffold System for Easy in Vitro Coimmobilization
RT of Biocatalytic Cascade Enzymes.";
RL ACS Catal. 8:5611-5620(2018).
RN [12]
RP FUNCTION.
RC STRAIN=SL1344;
RX PubMed=29531136; DOI=10.1128/iai.00172-18;
RA Anderson C.J., Satkovich J., Koeseoglu V.K., Agaisse H., Kendall M.M.;
RT "The Ethanolamine Permease EutH Promotes Vacuole Adaptation of Salmonella
RT enterica and Listeria monocytogenes during Macrophage Infection.";
RL Infect. Immun. 86:0-0(2018).
CC -!- FUNCTION: Probably a major component of the bacterial microcompartment
CC (BMC) shell dedicated to ethanolamine degradation (PubMed:22428024,
CC PubMed:27063436). Each homohexamer has a central pore with an opening
CC of up to 8.6 Angstroms. A positively-charged funnel leads to the pore
CC from each side of the hexamer. The pore probably allows metabolite
CC passage into and out of the BMC (By similarity). Expression of eutK,
CC eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a
CC single BMC. Expression alone leads to thick filaments that interfere
CC with cell separation (PubMed:22428024, PubMed:27063436). Coexpression
CC of eutQ with eutSMNLK permits E.coli to make cells with more than one
CC mobile BMC, as is usual in vivo. May play a role in BMC shell
CC biogenesis (PubMed:27063436). Can replace homolog pduA in the pdu
CC operon, cells grow better than wild-type on 1,2-propanediol and vitamin
CC B12. Protein is incorporated into the pdu BMC microcompartment
CC (PubMed:28585808). {ECO:0000250|UniProtKB:P0ABF4,
CC ECO:0000269|PubMed:22428024, ECO:0000269|PubMed:27063436,
CC ECO:0000269|PubMed:28585808}.
CC -!- FUNCTION: The ethanolamine (EA) catabolic bacterial microcompartment
CC (BMC) probably concentrates low levels of ethanolamine catabolic
CC enzymes, concentrates volatile reaction intermediates, keeps the level
CC of toxic acetaldehyde low, generates enough acetyl-CoA to support cell
CC growth, and maintains a pool of free coenzyme A (CoA) and NAD
CC (Probable) (PubMed:16585748). Deletion of BMC genes (eutK, eutL, eutM)
CC restores growth of eutD deletions, suggesting there are dedicated pools
CC of coenzyme A (CoA) and NAD in the BMC (PubMed:23585538).
CC {ECO:0000269|PubMed:16585748, ECO:0000269|PubMed:23585538,
CC ECO:0000305|PubMed:16291677, ECO:0000305|PubMed:23585538,
CC ECO:0000305|PubMed:7868611}.
CC -!- FUNCTION: Expression of the eut operon allows this bacteria to use
CC ethanolamine as a carbon, nitrogen and energy source. It relies on
CC cobalamin (vitamin B12) both as a cofactor for the ethanolamine
CC ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078).
CC EA enhances bacterial survival in macrophages in a concentration-
CC dependent manner, suggesting it is an important nutrient during
CC infection (PubMed:29531136). {ECO:0000269|PubMed:29531136,
CC ECO:0000269|PubMed:3045078}.
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000269|PubMed:3045078}.
CC -!- SUBUNIT: Homohexamer with a central pore of up to 8.6 Angstroms
CC diameter. The hexamers pack into a two-dimensional array (By
CC similarity). Interacts with EutQ; a probably cytoplasm-facing helix
CC (Val-49 to Gln-64) interacts with N-terminus of EutQ (PubMed:27063436).
CC {ECO:0000250|UniProtKB:P0ABF4, ECO:0000269|PubMed:27063436}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:27063436, ECO:0000305|PubMed:28585808}.
CC -!- INDUCTION: Part of the 17-gene eut operon transcribed from a single
CC promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl,
CC vitamin B12). {ECO:0000269|PubMed:3045078}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted when the 17-gene
CC operon is otherwise intact, possibly due to polar effects on downstream
CC genes (PubMed:7868611). Not required for cobalamin-dependent
CC degradation of ethanolamine (EA) when polar effects are removed. A
CC double eutD-eutM deletion is also not required for growth in the above
CC conditions (PubMed:10464203). A double eutM-eutN strain grows as well
CC as wild-type on EA and cyanocobalamin, but a quadruple eutL-eutK eutM-
CC eutN strain does not grow (PubMed:16291677). A non-polar deletion
CC mutant grows on EA at pH 5.5 to pH 7.0 but not at pH 8.0 or pH 8.5,
CC releases increased amounts of acetaldehyde on EA plus vitamin B12.
CC Preventing acetaldehyde vapor loss allows growth up to pH 8.5
CC (PubMed:16585748). {ECO:0000269|PubMed:10464203,
CC ECO:0000269|PubMed:16291677, ECO:0000269|PubMed:16585748,
CC ECO:0000269|PubMed:7868611}.
CC -!- BIOTECHNOLOGY: Artificial BMCs can be made in E.coli by expressing
CC eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins
CC can be targeted to them and beta-galactosidase (lacZ) was active within
CC the BMC, showing the BMC allows passage of substrate into the interior.
CC This can lead to the development of tailored BMCs for specific
CC metabolic reactions (PubMed:22428024, PubMed:27063436). The addition of
CC eutQ to the eutSMNLK construct results in biogenesis of multiple BMCs
CC (PubMed:27063436). Can incorporate into the pdu BMC where it alters
CC growth, suggesting fine-tuning metabolite flux by using different BMC
CC components is possible (PubMed:28585808). {ECO:0000269|PubMed:22428024,
CC ECO:0000269|PubMed:27063436, ECO:0000269|PubMed:28585808}.
CC -!- BIOTECHNOLOGY: Can be used as a self-assembling protein scaffold for
CC synthetic biology. Overexpressed, purified protein with a SpyCatcher
CC tag added to the C-terminus yields self-assembling fibrils that are
CC stable at pH 5-9 and up to 50 degrees Celsius. Addition of SpyTagged
CC cargo proteins leads to isopeptide bond formation between the scaffold
CC and cargo proteins, colocalizing and stabilizing the cargo proteins and
CC reducing the time for the reaction to make maximimal product.
CC {ECO:0000269|Ref.11}.
CC -!- MISCELLANEOUS: The need for a bacterial microcompartment in EA
CC metabolism can be bypassed by increasing the levels of EAL and an
CC acetaldehyde dehydrogenase (not necessarily EutE).
CC {ECO:0000269|PubMed:16291677}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01278, ECO:0000305|PubMed:10464203}.
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DR EMBL; U18560; AAA80207.1; -; Genomic_DNA.
DR EMBL; AF093749; AAC78116.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21359.1; -; Genomic_DNA.
DR RefSeq; NP_461400.1; NC_003197.2.
DR RefSeq; WP_000387716.1; NC_003197.2.
DR AlphaFoldDB; P41791; -.
DR SMR; P41791; -.
DR STRING; 99287.STM2465; -.
DR PaxDb; P41791; -.
DR EnsemblBacteria; AAL21359; AAL21359; STM2465.
DR GeneID; 1253987; -.
DR KEGG; stm:STM2465; -.
DR PATRIC; fig|99287.12.peg.2603; -.
DR HOGENOM; CLU_064903_5_3_6; -.
DR OMA; QFREGVN; -.
DR PhylomeDB; P41791; -.
DR BioCyc; SENT99287:STM2465-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031471; C:ethanolamine degradation polyhedral organelle; IDA:UniProtKB.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
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 Pfam; PF00936; BMC; 1.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; SSF143414; 1.
DR PROSITE; PS01139; BMC_1; 1.
DR PROSITE; PS51930; BMC_2; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Reference proteome; Virulence.
FT CHAIN 1..96
FT /note="Bacterial microcompartment shell protein EutM"
FT /id="PRO_0000004787"
FT DOMAIN 3..87
FT /note="BMC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT MUTAGEN 24
FT /note="K->A: No longer complements pduA in the pdu operon."
FT /evidence="ECO:0000269|PubMed:28585808"
FT MUTAGEN 49
FT /note="V->S: Still interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 50..60
FT /note="AACKAATDAGA->SACKSATDSGS: Still interacts with
FT EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 53
FT /note="K->A: Still interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 53
FT /note="K->D: No longer interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 54
FT /note="A->S: Still interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 57
FT /note="D->A,K: No longer interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 58
FT /note="A->S: Still interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 61
FT /note="A->S: Still interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 64
FT /note="Q->A,D: Still interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 64
FT /note="Q->K: No longer interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
FT MUTAGEN 65
FT /note="R->A: Still interacts with EutQ."
FT /evidence="ECO:0000269|PubMed:27063436"
SQ SEQUENCE 96 AA; 9843 MW; 01710D8ABB8CF6BC CRC64;
MEALGMIETR GLVALIEASD AMVKAARVKL VGVKQIGGGL CTAMVRGDVA ACKAATDAGA
AAAQRIGELV SVHVIPRPHG DLEEVFPISF KGDSNI
