BMCT1_HALO1
ID BMCT1_HALO1 Reviewed; 205 AA.
AC D0LHE3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Bacterial microcompartment protein trimer-1;
DE Short=BMC-T1 {ECO:0000303|PubMed:28642439};
DE Short=BMC-T1(S) {ECO:0000303|PubMed:30833088};
GN OrderedLocusNames=Hoch_5812;
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]
RP SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RX PubMed=31075444; DOI=10.1016/j.ymben.2019.04.011;
RA Ferlez B., Sutter M., Kerfeld C.A.;
RT "A designed bacterial microcompartment shell with tunable composition and
RT precision cargo loading.";
RL Metab. Eng. 54:286-291(2019).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY OF BMC, FUNCTION, SUBUNIT, SUBCELLULAR
RP 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 [5] {ECO:0007744|PDB:5DIH, ECO:0007744|PDB:5DII}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), SUBUNIT, BIOTECHNOLOGY, AND
RP MUTAGENESIS OF SER-55.
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2;
RX PubMed=26704697; DOI=10.1021/jacs.5b11734;
RA Aussignargues C., Pandelia M.E., Sutter M., Plegaria J.S., Zarzycki J.,
RA Turmo A., Huang J., Ducat D.C., Hegg E.L., Gibney B.R., Kerfeld C.A.;
RT "Structure and Function of a Bacterial Microcompartment Shell Protein
RT Engineered to Bind a [4Fe-4S] Cluster.";
RL J. Am. Chem. Soc. 138:5262-5270(2016).
RN [6] {ECO:0007744|PDB:6N06, ECO:0007744|PDB:6N0F, ECO:0007744|PDB:6N0G}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF BMC, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
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. This protein does not
CC form stacked pseudohexamers in the BMC. There are 20 BMC-T
CC pseudohexamers per BMC, composed of mixed BMC-T1, BMC-T2 and BMC-T3.
CC The shell facets are 20-30 Angstroms thick, with 1 of BMC-T trimers
CC protruding to the exterior. {ECO:0000269|PubMed:28642439,
CC ECO:0000269|PubMed:30833088}.
CC -!- SUBUNIT: Homotrimerizes to form a pseudohexamer (PubMed:28642439,
CC PubMed:30833088, PubMed:26704697). Unlike its paralogs BMC-T2 and BMC-
CC T3, the pseudohexamers do not stack. The concave side faces outward,
CC with the N- and C-terminii exposed to the cytoplasm (PubMed:28642439,
CC PubMed:30833088). {ECO:0000269|PubMed:26704697,
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, ECO:0000269|PubMed:31075444}.
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.
CC {ECO:0000269|PubMed:28642439}.
CC -!- DISRUPTION PHENOTYPE: 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 >10-fold decrease in BMC shells 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 (PubMed:24631000, PubMed:28642439). BMC-H can be modified to
CC place its N- and C-terminii in the interior of the shell (called CPH).
CC Fusing proteins to the C-terminus of CPH allows targeting of cargo
CC proteins to the lumen of the organelle composed of CPH, BMC-P and BMC-
CC T1 (PubMed:31075444). This subunit has been modifed to bind a 4Fe-4S
CC center, which is the first step in conferring electron-transfer
CC function to BMCs (PubMed:26704697). {ECO:0000269|PubMed:24631000,
CC ECO:0000269|PubMed:26704697, ECO:0000269|PubMed:28642439,
CC ECO:0000269|PubMed:31075444}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01278}.
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DR EMBL; CP001804; ACY18288.1; -; Genomic_DNA.
DR RefSeq; WP_012830880.1; NC_013440.1.
DR PDB; 5DIH; X-ray; 2.44 A; A/B/C/D/E/F=1-205.
DR PDB; 5DII; X-ray; 1.80 A; A/B/C/D/E/F=1-205.
DR PDB; 6N06; EM; 3.40 A; A/B/C=1-205.
DR PDB; 6N0F; EM; 3.90 A; G/H/I/M/N/O/S/T/U=1-205.
DR PDB; 6N0G; EM; 3.60 A; A/B/C=1-205.
DR PDBsum; 5DIH; -.
DR PDBsum; 5DII; -.
DR PDBsum; 6N06; -.
DR PDBsum; 6N0F; -.
DR PDBsum; 6N0G; -.
DR AlphaFoldDB; D0LHE3; -.
DR SMR; D0LHE3; -.
DR IntAct; D0LHE3; 1.
DR STRING; 502025.Hoch_5812; -.
DR EnsemblBacteria; ACY18288; ACY18288; Hoch_5812.
DR KEGG; hoh:Hoch_5812; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_115793_0_0_7; -.
DR OMA; VVETWSV; -.
DR OrthoDB; 1759482at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR Gene3D; 3.30.70.1710; -; 2.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR044872; CcmK/CsoS1_BMC.
DR InterPro; IPR011238; Organelle_shell_prot_PduT.
DR Pfam; PF00936; BMC; 2.
DR PIRSF; PIRSF034834; PduT; 1.
DR SMART; SM00877; BMC; 2.
DR SUPFAM; SSF143414; SSF143414; 2.
DR PROSITE; PS51930; BMC_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Reference proteome.
FT CHAIN 1..205
FT /note="Bacterial microcompartment protein trimer-1"
FT /id="PRO_0000452546"
FT DOMAIN 21..106
FT /note="BMC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT DOMAIN 120..204
FT /note="BMC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 52
FT /note="Gating residue"
FT /evidence="ECO:0000305|PubMed:30833088"
FT MUTAGEN 55
FT /note="S->C: Binds a 4Fe-4S cluster, exposed on the concave
FT face."
FT /evidence="ECO:0000269|PubMed:26704697"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:5DII"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:5DII"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:5DII"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:5DII"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:5DII"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:5DII"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:5DII"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5DIH"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:5DII"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:5DII"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5DII"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5DII"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:5DII"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:5DII"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:5DII"
FT TURN 154..158
FT /evidence="ECO:0007829|PDB:5DII"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:5DII"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:5DII"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5DII"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:5DII"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:5DII"
SQ SEQUENCE 205 AA; 21900 MW; 96E7ED7A46105E0C CRC64;
MDHAPERFDA TPPAGEPDRP ALGVLELTSI ARGITVADAA LKRAPSLLLM SRPVSSGKHL
LMMRGQVAEV EESMIAAREI AGAGSGALLD ELELPYAHEQ LWRFLDAPVV ADAWEEDTES
VIIVETATVC AAIDSADAAL KTAPVVLRDM RLAIGIAGKA FFTLTGELAD VEAAAEVVRE
RCGARLLELA CIARPVDELR GRLFF
