EUTS_CLOD6
ID EUTS_CLOD6 Reviewed; 116 AA.
AC Q187M0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Bacterial microcompartment shell protein EutS;
DE AltName: Full=Ethanolamine utilization protein EutS;
GN Name=eutS; Synonyms=CD1908; OrderedLocusNames=CD630_19080;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
RN [2] {ECO:0007744|PDB:4AXI}
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 2-116, FUNCTION, SUBUNIT, AND
RP PROBABLE SUBCELLULAR LOCATION.
RC STRAIN=630;
RX PubMed=23144756; DOI=10.1371/journal.pone.0048360;
RA Pitts A.C., Tuck L.R., Faulds-Pain A., Lewis R.J., Marles-Wright J.;
RT "Structural insight into the Clostridium difficile ethanolamine utilisation
RT microcompartment.";
RL PLoS ONE 7:e48360-e48360(2012).
CC -!- FUNCTION: A component of the bacterial microcompartment (BMC) shell
CC dedicated to ethanolamine degradation. Expression of the eut operon may
CC allow this bacteria to use ethanolamine as a carbon, nitrogen and
CC energy source (Probable). Unlike its S.typhimurium homolog, does not
CC make BMCs when expressed in E.coli (PubMed:23144756). Targets at least
CC 2 proteins (EutC and EutE) to the interior of the BMC (By similarity).
CC Proteins such as EutS containing circularly permuted BMC domains may
CC play a key role in conferring heterogeneity and flexibility in this BMC
CC (Probable). {ECO:0000250|UniProtKB:Q9ZFV7, ECO:0000269|PubMed:23144756,
CC ECO:0000305, ECO:0000305|PubMed:23144756}.
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000305|PubMed:23144756}.
CC -!- SUBUNIT: Homohexamer; unlike its E.coli ortholog the hexamer is flat.
CC Its pore of about 10 Angstroms in diameter is closed in the crystal
CC structure (PubMed:23144756). Interacts with the N-terminus of EutC and
CC of EutE, targeting them to the interior of the BMC (By similarity).
CC {ECO:0000250|UniProtKB:Q9ZFV7, ECO:0000269|PubMed:23144756}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:23144756}.
CC -!- SIMILARITY: Belongs to the EutS/PduU family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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; AM180355; CAJ68784.1; -; Genomic_DNA.
DR RefSeq; WP_003423973.1; NZ_CP010905.2.
DR RefSeq; YP_001088415.1; NC_009089.1.
DR PDB; 4AXI; X-ray; 1.51 A; A/B=2-116.
DR PDBsum; 4AXI; -.
DR AlphaFoldDB; Q187M0; -.
DR SMR; Q187M0; -.
DR STRING; 272563.CD630_19080; -.
DR EnsemblBacteria; CAJ68784; CAJ68784; CD630_19080.
DR GeneID; 66354289; -.
DR KEGG; cdf:CD630_19080; -.
DR KEGG; pdc:CDIF630_02112; -.
DR PATRIC; fig|272563.120.peg.2004; -.
DR eggNOG; COG4810; Bacteria.
DR OMA; HIIPNPQ; -.
DR PhylomeDB; Q187M0; -.
DR BioCyc; PDIF272563:G12WB-2052-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0046336; P:ethanolamine 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 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Reference proteome.
FT CHAIN 1..116
FT /note="Bacterial microcompartment shell protein EutS"
FT /id="PRO_0000452914"
FT DOMAIN 8..108
FT /note="BMC circularly permuted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4AXI"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:4AXI"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:4AXI"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:4AXI"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:4AXI"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:4AXI"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:4AXI"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:4AXI"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:4AXI"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:4AXI"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4AXI"
SQ SEQUENCE 116 AA; 12408 MW; 0542FB4D23FF0BCD CRC64;
MTEESKQRVI QEYVPGKQVT LAHIIANPNE DIYKKLGLVL DKKDAIGILT ITPSEASIIA
ADVATKASNV SLGFIDRFSG SVVISGDVSS VESALNDVLE VLGNMLNFSS TKITRT
