BMCT3_HALO1
ID BMCT3_HALO1 Reviewed; 206 AA.
AC D0LV02;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Bacterial microcompartment protein trimer-3;
DE Short=BMC-T3 {ECO:0000303|PubMed:28642439};
DE Short=BMC-T3(D) {ECO:0000303|PubMed:30833088};
GN OrderedLocusNames=Hoch_3341;
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Nannocystineae; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2;
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
RN [2]
RP EXPRESSION IN E.COLI, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP BIOTECHNOLOGY.
RX PubMed=24631000; DOI=10.1016/j.jmb.2014.02.025;
RA Lassila J.K., Bernstein S.L., Kinney J.N., Axen S.D., Kerfeld C.A.;
RT "Assembly of robust bacterial microcompartment shells using building blocks
RT from an organelle of unknown function.";
RL J. Mol. Biol. 426:2217-2228(2014).
RN [3] {ECO:0007744|PDB:5V76}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), STRUCTURE BY ELECTRON MICROSCOPY OF
RP BMC, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2;
RX PubMed=28642439; DOI=10.1126/science.aan3289;
RA Sutter M., Greber B., Aussignargues C., Kerfeld C.A.;
RT "Assembly principles and structure of a 6.5-MDa bacterial microcompartment
RT shell.";
RL Science 356:1293-1297(2017).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=30833088; DOI=10.1016/j.str.2019.01.017;
RA Greber B.J., Sutter M., Kerfeld C.A.;
RT "The Plasticity of Molecular Interactions Governs Bacterial
RT Microcompartment Shell Assembly.";
RL Structure 27:749-763.e4(2019).
CC -!- FUNCTION: A minor component of the bacterial microcompartment (BMC)
CC shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P
CC (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms 40 nm
CC artificial BMCs with a molecular mass of 6.5 MDa. One of 2 stacked
CC pseudohexamers in the BMC. There are 20 BMC-T pseudohexamers per BMC,
CC composed of mixed BMC-T1, BMC-T2 and BMC-T3. The shell facets are 20-30
CC Angstroms thick, with 1 of the stacked BMC-T trimers protruding to the
CC exterior (PubMed:28642439, PubMed:30833088). The stacked trimers may
CC serve as conduits to allow metabolite flux across the protein shell,
CC gated by Arg-68 which contacts Glu-67 in an adjacent subunit; they are
CC flexible enough to play a role in accommodating variations in shell
CC assembly (Probable). {ECO:0000269|PubMed:28642439,
CC ECO:0000269|PubMed:30833088, ECO:0000305|PubMed:30833088}.
CC -!- SUBUNIT: Homotrimerizes to form a pseudohexamer. These stack, with the
CC concave faces together, with the concave faces together, in purified
CC bacterial microcompartments (BMC). {ECO:0000269|PubMed:28642439}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:24631000, ECO:0000269|PubMed:28642439,
CC ECO:0000269|PubMed:30833088}.
CC -!- DOMAIN: These proteins have 2 BMC domains which evolve independently of
CC each other, giving the term pseudohexamer to the trimerized subunit.
CC Although the homotrimer fills the approximate space of a BMC hexamer
CC protein, the BMC-T trimers are more compact. Their universal presence
CC in BMCs indicates their structural importance. The homohexamers form
CC pores of at least 5 Angstroms in diameter; in the stacked homohexamer
CC both pores are closed (PubMed:28642439). In the BMC the inner pore is
CC fully or partially closed while the outer pore is closed
CC (PubMed:30833088). {ECO:0000269|PubMed:28642439,
CC ECO:0000269|PubMed:30833088}.
CC -!- DISRUPTION PHENOTYPE: Not required for efficient BMC formation; when
CC deleted from an artificial operon (Hoch_5815, Hoch_5812, Hoch_3341,
CC Hoch_5816, Hoch_4425, Hoch_4426, Hoch_5814) being expressed in E.coli,
CC a 2-fold decrease in BMC formation is seen.
CC {ECO:0000269|PubMed:24631000}.
CC -!- BIOTECHNOLOGY: Artificial BMCs can be made in E.coli by expressing
CC (Hoch_5815, Hoch_5812, Hoch_3341, Hoch_5816, Hoch_4425, Hoch_4426,
CC Hoch_5814) or (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T
CC (Hoch_5812, Hoch_5816, Hoch_3341)). Cargo proteins can be targeted to
CC this BMC. {ECO:0000269|PubMed:24631000, ECO:0000269|PubMed:28642439}.
CC -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC ProRule:PRU01279}.
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DR EMBL; CP001804; ACY15843.1; -; Genomic_DNA.
DR RefSeq; WP_012828443.1; NC_013440.1.
DR PDB; 5V76; X-ray; 1.55 A; A/B=1-206.
DR PDBsum; 5V76; -.
DR AlphaFoldDB; D0LV02; -.
DR SMR; D0LV02; -.
DR IntAct; D0LV02; 1.
DR STRING; 502025.Hoch_3341; -.
DR EnsemblBacteria; ACY15843; ACY15843; Hoch_3341.
DR KEGG; hoh:Hoch_3341; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_091281_0_0_7; -.
DR OMA; YEMAPAL; -.
DR OrthoDB; 1374667at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR Gene3D; 3.30.70.1710; -; 2.
DR InterPro; IPR044870; BMC_CP.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; SSF143414; 1.
DR PROSITE; PS51931; BMC_CP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Reference proteome.
FT CHAIN 1..206
FT /note="Bacterial microcompartment protein trimer-3"
FT /id="PRO_0000452548"
FT DOMAIN 2..104
FT /note="BMC circularly permuted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT DOMAIN 105..206
FT /note="BMC circularly permuted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT MOTIF 67..68
FT /note="Pore gating residues"
FT /evidence="ECO:0000269|PubMed:30833088,
FT ECO:0000305|PubMed:28642439, ECO:0007744|PDB:5V76"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:5V76"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:5V76"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5V76"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:5V76"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5V76"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:5V76"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5V76"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:5V76"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:5V76"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:5V76"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:5V76"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:5V76"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:5V76"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5V76"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:5V76"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:5V76"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:5V76"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:5V76"
SQ SEQUENCE 206 AA; 21851 MW; 95D3F41ABB61CC8D CRC64;
MELRAYTVLD ALQPQLVAFL QTVSTGFMPM EQQASVLVEI APGIAVNQLT DAALKATRCQ
PGLQIVERAY GLIEMHDDDQ GQVRAAGDAM LAHLGAREAD RLAPRVVSSQ IITGIDGHQS
QLINRMRHGD MIQAGQTLYI LEVHPAGYAA LAANEAEKAA PIKLLEVVTF GAFGRLWLGG
GEAEIAEAAR AAEGALAGLS GRDNRG
