EUTM_CLOD6
ID EUTM_CLOD6 Reviewed; 95 AA.
AC Q187N0;
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 EutM {ECO:0000305|PubMed:23144756};
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:23144756};
GN Synonyms=CD1918, eutK {ECO:0000303|PubMed:16804543};
GN OrderedLocusNames=CD630_19180;
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:4AXJ}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 2-95, 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. Each homohexamer has a central
CC pore with an opening of up to 9.0 Angstroms. Expression of the eut
CC operon may allow this bacteria to use ethanolamine as a carbon,
CC nitrogen and energy source. The pore probably allows metabolite passage
CC into and out of the BMC. {ECO:0000305|PubMed:23144756}.
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000305|PubMed:23144756}.
CC -!- SUBUNIT: Homohexamer; has a positively charged pore 9 Angstroms in
CC diameter. The hexamers pack into a two-dimensional array
CC (PubMed:23144756). May interact with EutQ (By similarity).
CC {ECO:0000250|UniProtKB:P41791, ECO:0000269|PubMed:23144756}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:23144756}.
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; AM180355; CAJ68794.1; -; Genomic_DNA.
DR RefSeq; WP_003423991.1; NZ_CP010905.2.
DR RefSeq; YP_001088425.1; NC_009089.1.
DR PDB; 4AXJ; X-ray; 1.62 A; A/B/C=2-95.
DR PDBsum; 4AXJ; -.
DR AlphaFoldDB; Q187N0; -.
DR SMR; Q187N0; -.
DR STRING; 272563.CD630_19180; -.
DR EnsemblBacteria; CAJ68794; CAJ68794; CD630_19180.
DR GeneID; 66354299; -.
DR KEGG; cdf:CD630_19180; -.
DR KEGG; pdc:CDIF630_02122; -.
DR PATRIC; fig|272563.120.peg.2014; -.
DR eggNOG; COG4577; Bacteria.
DR OMA; QFREGVN; -.
DR PhylomeDB; Q187N0; -.
DR BioCyc; PDIF272563:G12WB-2062-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 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 3D-structure; Bacterial microcompartment; Reference proteome.
FT CHAIN 1..95
FT /note="Bacterial microcompartment shell protein EutM"
FT /id="PRO_0000452912"
FT DOMAIN 6..90
FT /note="BMC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:4AXJ"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:4AXJ"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4AXJ"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:4AXJ"
FT HELIX 52..69
FT /evidence="ECO:0007829|PDB:4AXJ"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:4AXJ"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:4AXJ"
SQ SEQUENCE 95 AA; 9488 MW; 3474016F3283EAD5 CRC64;
MASANALGMI ETKGLVGAIE AADAMVKAAN VQLVGKEQVG GGLVTVMVRG DVGAVKAATD
AGAAAAERVG ELISVHVIPR PHFEVDAILP KVSAE