BMCT2_HALO1
ID BMCT2_HALO1 Reviewed; 212 AA.
AC D0LID6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Bacterial microcompartment protein trimer-2;
DE Short=BMC-T2 {ECO:0000303|PubMed:28642439};
DE Short=BMC-T2(D) {ECO:0000303|PubMed:30833088};
GN OrderedLocusNames=Hoch_5816;
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:5V74, ECO:0007744|PDB:5V75}
RP X-RAY CRYSTALLOGRAPHY (1.70 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] {ECO:0007744|PDB:6MZU, ECO:0007744|PDB:6MZV, ECO:0007744|PDB:6MZX, ECO:0007744|PDB:6MZY}
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 chemical flux across the protein shell,
CC gated by Arg-70 which contacts Glu-69 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, in purified bacterial microcompartments (BMC).
CC {ECO:0000269|PubMed:28642439, ECO:0000269|PubMed:30833088}.
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 at least 5 Angstroms in diameter; in the stacked homohexamer 1
CC pore is open and the other is closed (PubMed:28642439). In the BMC the
CC inner pore is 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 normal BMC shells form. {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; ACY18292.1; -; Genomic_DNA.
DR RefSeq; WP_012830884.1; NC_013440.1.
DR PDB; 5V74; X-ray; 3.51 A; 18/19/28/29/38/39/48/49/A8/A9/B8/B9/C8/C9/D8/D9/E8/E9/F8/F9/G8/G9/H8/H9/I8/I9/J8/J9/K8/K9=1-212.
DR PDB; 5V75; X-ray; 1.70 A; A/B/C/D/E/F=1-212.
DR PDB; 6MZU; EM; 3.40 A; A/B/C/D/E/F=1-212.
DR PDB; 6MZV; EM; 3.40 A; A/B/C/D/E/F=1-212.
DR PDB; 6MZX; EM; 3.00 A; A8/A9=1-212.
DR PDB; 6MZY; EM; 3.30 A; A8/A9=1-212.
DR PDB; 6N07; EM; 3.60 A; A/B/C/D/E/F=1-205.
DR PDB; 6N09; EM; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-212.
DR PDB; 6N0F; EM; 3.90 A; A/B/C/D/E/F=1-212.
DR PDB; 6N0G; EM; 3.60 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-212.
DR PDBsum; 5V74; -.
DR PDBsum; 5V75; -.
DR PDBsum; 6MZU; -.
DR PDBsum; 6MZV; -.
DR PDBsum; 6MZX; -.
DR PDBsum; 6MZY; -.
DR PDBsum; 6N07; -.
DR PDBsum; 6N09; -.
DR PDBsum; 6N0F; -.
DR PDBsum; 6N0G; -.
DR AlphaFoldDB; D0LID6; -.
DR SMR; D0LID6; -.
DR IntAct; D0LID6; 1.
DR STRING; 502025.Hoch_5816; -.
DR EnsemblBacteria; ACY18292; ACY18292; Hoch_5816.
DR KEGG; hoh:Hoch_5816; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_091281_0_0_7; -.
DR OMA; WIEVAPG; -.
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 Pfam; PF00936; BMC; 1.
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..212
FT /note="Bacterial microcompartment protein trimer-2"
FT /id="PRO_0000452547"
FT DOMAIN 4..106
FT /note="BMC circularly permuted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT DOMAIN 107..211
FT /note="BMC circularly permuted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT MOTIF 69..70
FT /note="Pore gating residues"
FT /evidence="ECO:0000269|PubMed:30833088,
FT ECO:0000305|PubMed:28642439, ECO:0007744|PDB:5V75"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:5V75"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:5V75"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:5V75"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:5V75"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5V75"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:5V75"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5V75"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:5V75"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:5V75"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5V75"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:5V75"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:5V75"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:5V75"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5V75"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:5V75"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5V75"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:5V75"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:5V75"
SQ SEQUENCE 212 AA; 22882 MW; 44131513233029A3 CRC64;
MSITLRTYIF LDALQPQLAT FIGKTARGFL PVPGQASLWV EIAPGIAINR VTDAALKATK
VQPAVQVVER AYGLLEVHHF DQGEVLAAGS TILDKLEVRE EGRLKPQVMT HQIIRAVEAY
QTQIINRNSQ GMMILPGESL FILETQPAGY AVLAANEAEK AANVHLVNVT PYGAFGRLYL
AGSEAEIDAA AEAAEAAIRS VSGVAQESFR DR
