CUTR_STRIS
ID CUTR_STRIS Reviewed; 116 AA.
AC A0A0E2IV13;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Bacterial microcompartment shell protein CutR {ECO:0000303|PubMed:32885887};
DE AltName: Full=Bacterial microcompartment protein homohexamer {ECO:0000305};
DE Short=BMC-H {ECO:0000305};
DE AltName: Full=Propanediol utilization protein CutR;
GN Name=cutR {ECO:0000303|PubMed:32885887}; ORFNames=HMPREF1654_00416;
OS Streptococcus intermedius (strain ATCC 27335 / DSM 20573 / CCUG 32759 / CIP
OS 103248 / JCM 12996 / LMG 17840 / NCTC 11324 / SK54 / 1877).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1095731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27335 / DSM 20573 / CCUG 32759 / CIP 103248 / JCM 12996 / LMG
RC 17840 / NCTC 11324 / SK54 / 1877;
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Leonetti C., Kirega A.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Streptococcus intermedius ATCC 27335.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:6XPH, ECO:0007744|PDB:6XPI, ECO:0007744|PDB:6XPJ, ECO:0007744|PDB:6XPK, ECO:0007744|PDB:6XPL}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTATED PROTEINS, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=32885887; DOI=10.1002/pro.3941;
RA Ochoa J.M., Nguyen V.N., Nie M., Sawaya M.R., Bobik T.A., Yeates T.O.;
RT "Symmetry breaking and structural polymorphism in a bacterial
RT microcompartment shell protein for choline utilization.";
RL Protein Sci. 29:2201-2212(2020).
CC -!- FUNCTION: A minor shell protein of the choline degradation-specific
CC bacterial microcompartment (BMC). Proteins such as this one with
CC circularly permuted BMC domains may play a key role in conferring
CC heterogeneity and flexibility in this BMC.
CC {ECO:0000305|PubMed:32885887}.
CC -!- PATHWAY: Amine and polyamine metabolism; choline degradation.
CC {ECO:0000305|PubMed:32885887}.
CC -!- SUBUNIT: Has been crystallized in 5 structures (all are mutated, 3 have
CC an N-terminal His-tag), most are homohexameric with a central pore. In
CC two the homohexamer lies flat with a beta-barrel on the flat face
CC created by the protruding N termini of the six chains
CC (PubMed:32885887). In 2 others the hexamer is not flat but has a six-
CC fold screw axis; the screw pitch is 33.8 or 41.9 Angstroms depending on
CC the structure (PubMed:32885887). Interacts with the BMC major shell
CC protein (By similarity). {ECO:0000250|UniProtKB:P0DUV8,
CC ECO:0000269|PubMed:32885887, ECO:0007744|PDB:6XPI,
CC ECO:0007744|PDB:6XPJ, ECO:0007744|PDB:6XPK, ECO:0007744|PDB:6XPL}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:32885887}.
CC -!- DOMAIN: One side of the hexamer is concave and lined by hydrophobic
CC residues, the other side has a slightly protruding, 6-stranded beta-
CC barrel. {ECO:0000269|PubMed:32885887}.
CC -!- SIMILARITY: Belongs to the EutS/PduU family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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DR EMBL; ATFK01000001; EPH05253.1; -; Genomic_DNA.
DR RefSeq; WP_004234014.1; NZ_ATFK01000001.1.
DR PDB; 6XPH; X-ray; 1.80 A; A/B=1-116.
DR PDB; 6XPI; X-ray; 2.60 A; A/B/C/D/E/F=1-116.
DR PDB; 6XPJ; X-ray; 1.50 A; A/B/C=1-116.
DR PDB; 6XPK; X-ray; 2.80 A; A=1-116.
DR PDB; 6XPL; X-ray; 3.30 A; A=1-116.
DR PDBsum; 6XPH; -.
DR PDBsum; 6XPI; -.
DR PDBsum; 6XPJ; -.
DR PDBsum; 6XPK; -.
DR PDBsum; 6XPL; -.
DR SMR; A0A0E2IV13; -.
DR EnsemblBacteria; EPH05253; EPH05253; HMPREF1654_00416.
DR GeneID; 57844526; -.
DR PATRIC; fig|1316583.3.peg.414; -.
DR UniPathway; UPA01069; -.
DR Proteomes; UP000014618; Unassembled WGS sequence.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR Gene3D; 3.30.70.1710; -; 1.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Transport.
FT CHAIN 1..116
FT /note="Bacterial microcompartment shell protein CutR"
FT /id="PRO_0000454249"
FT DOMAIN 10..108
FT /note="BMC circularly permuted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT HELIX 1..6
FT /evidence="ECO:0007829|PDB:6XPJ"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:6XPJ"
FT STRAND 20..29
FT /evidence="ECO:0007829|PDB:6XPJ"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:6XPJ"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:6XPJ"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6XPJ"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:6XPJ"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6XPJ"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:6XPJ"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:6XPJ"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:6XPJ"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6XPJ"
SQ SEQUENCE 116 AA; 12369 MW; 651922761A250B8C CRC64;
MIEELGKIDR IIQESVPGKQ ITLAHVIAAP IEAVYECLGV DHEGAIGVVS LTPNETAIIA
ADIAGKAANI DICFVDRFTG SVMFSGDIQS VETSLEDILE YFKNSLGFST VPLTKS
