BMCH_HALO1
ID BMCH_HALO1 Reviewed; 99 AA.
AC D0LID5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Bacterial microcompartment protein homohexamer {ECO:0000303|PubMed:26617073};
DE Short=BMC-H {ECO:0000303|PubMed:26617073};
GN OrderedLocusNames=Hoch_5815;
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:5DJB}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF LYS-28
RP AND ARG-78.
RX PubMed=26617073; DOI=10.1021/acs.nanolett.5b04259;
RA Sutter M., Faulkner M., Aussignargues C., Paasch B.C., Barrett S.,
RA Kerfeld C.A., Liu L.N.;
RT "Visualization of Bacterial Microcompartment Facet Assembly Using High-
RT Speed Atomic Force Microscopy.";
RL Nano Lett. 16:1590-1595(2016).
RN [4] {ECO:0007744|PDB:5V74}
RP X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS), STRUCTURE BY ELECTRON MICROSCOPY OF
RP BMC, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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:6NER}
RP X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, AND
RP BIOTECHNOLOGY.
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2;
RX PubMed=30901520; DOI=10.1021/acssynbio.9b00011;
RA Sutter M., McGuire S., Ferlez B., Kerfeld C.A.;
RT "Structural Characterization of a Synthetic Tandem-Domain Bacterial
RT Microcompartment Shell Protein Capable of Forming Icosahedral Shell
RT Assemblies.";
RL ACS Synth. Biol. 8:668-674(2019).
RN [6] {ECO:0007744|PDB:6NLU}
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 2-99, SUBCELLULAR LOCATION, AND
RP 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 [7] {ECO:0007744|PDB:6MZU, ECO:0007744|PDB:6MZV, ECO:0007744|PDB:6MZX, ECO:0007744|PDB:6N06, ECO:0007744|PDB:6N07, ECO:0007744|PDB:6N09, ECO:0007744|PDB:6N0F, ECO:0007744|PDB:6N0G}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 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: The only hexameric shell protein in this bacterium, it forms
CC the majority of the bacterial microcompartment (BMC) shell. Expression
CC of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3
CC BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms a 40 nm artificial BMC
CC with a molecular mass of 6.5 MDa. There are 60 BMC-H hexamers per BMC.
CC The shell facets are 20-30 Angstroms thick (a single hexamer layer),
CC with 1 of BMC-T trimers protruding to the exterior.
CC {ECO:0000269|PubMed:28642439, ECO:0000269|PubMed:30833088}.
CC -!- SUBUNIT: Homohexamer with a small central pore (PubMed:26617073,
CC PubMed:28642439, PubMed:31075444, PubMed:30833088) (Probable). When
CC purified protein is examined by atomic force microscopy it dynamically
CC makes uniform patches about 35 Angstroms thick with hexamers in the
CC same orientation (PubMed:26617073). In the BMC the concave side faces
CC outward, with the N- and C-terminii exposed to the cytoplasm
CC (PubMed:28642439). {ECO:0000269|PubMed:26617073,
CC ECO:0000269|PubMed:28642439, ECO:0000269|PubMed:30833088,
CC ECO:0000269|PubMed:31075444, ECO:0000305|PubMed:30901520}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:24631000, ECO:0000269|PubMed:28642439,
CC ECO:0000269|PubMed:30833088, ECO:0000269|PubMed:30901520,
CC ECO:0000269|PubMed:31075444}.
CC -!- DISRUPTION PHENOTYPE: Absolutely required for 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 no BMC shells are made. {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). Artificial BMCs can be
CC made by duplicating this gene with a 16 residue linker between the
CC copies (making an artificial BMC-T). The shell assembles into balls
CC with holes where the pentameric subunit would be, and can be used as a
CC model to study assembly and permeability (PubMed:30901520). Additional
CC changes to this protein place the N- and C-terminii in the interior of
CC the shell (called CPH). Fusing proteins to the C-terminus of CPH allows
CC targeting of cargo proteins to the lumen of the organelle composed of
CC CPH, BMC-P and BMC-T1 (PubMed:31075444). {ECO:0000269|PubMed:24631000,
CC ECO:0000269|PubMed:28642439, ECO:0000269|PubMed:30901520,
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; ACY18291.1; -; Genomic_DNA.
DR RefSeq; WP_012830883.1; NC_013440.1.
DR PDB; 5DJB; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-99.
DR PDB; 5V74; X-ray; 3.51 A; 12/13/14/15/16/17/22/23/24/25/26/27/32/33/34/35/36/37/42/43/44/45/46/47/A2/A3/A4/A5/A6/A7=1-99.
DR PDB; 6MZU; EM; 3.40 A; GA/GB/GC/GD/GE/GF/HA/HB/HC/HD/HE/HF/IA/IB/IC/ID/IE/IF/JA/JB/JC/JD/JE/JF/KA/KB/KC/KD/KE/KF=1-99.
DR PDB; 6MZV; EM; 3.40 A; GA/GB/GC/GD/GE/GF/HA/HB/HC/HD/HE/HF/IA/IB/IC/ID/IE/IF/JA/JB/JC/JD/JE/JF/KA/KB/KC/KD/KE/KF=1-99.
DR PDB; 6MZX; EM; 3.00 A; A2/A3/A4/A5/A6/A7=1-99.
DR PDB; 6MZY; EM; 3.30 A; A2/A3/A4/A5/A6/A7=1-99.
DR PDB; 6N06; EM; 3.40 A; GA/GB/GC/GD/GE/GF/HA/HB/HC/HD/HE/HF/IA/IB/IC/ID/IE/IF/JA/JB/JC/JD/JE/JF/KA/KB/KC/KD/KE/KF=1-99.
DR PDB; 6N07; EM; 3.60 A; GA/GB/GC/GD/GE/GF/HA/HB/HC/HD/HE/HF/IA/IB/IC/ID/IE/IF/JA/JB/JC/JD/JE/JF/KA/KB/KC/KD/KE/KF=1-99.
DR PDB; 6N09; EM; 3.50 A; GA/GB/GC/GD/GE/GF/HA/HB/HC/HD/HE/HF/IA/IB/IC/ID/IE/IF/JA/JB/JC/JD/JE/JF/KA/KB/KC/KD/KE/KF=1-99.
DR PDB; 6N0F; EM; 3.90 A; GA/GB/GC/GD/GE/GF/HA/HB/HC/HD/HE/HF/IA/IB/IC/ID/IE/IF/JA/JB/JC/JD/JE/JF/KA/KB/KC/KD/KE/KF=1-99.
DR PDB; 6N0G; EM; 3.60 A; GA/GB/GC/GD/GE/GF/HA/HB/HC/HD/HE/HF/IA/IB/IC/ID/IE/IF/JA/JB/JC/JD/JE/JF/KA/KB/KC/KD/KE/KF=1-99.
DR PDB; 6NER; X-ray; 3.59 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/Y/Z/a/b/c/d=1-99.
DR PDB; 6NLU; X-ray; 1.61 A; A/B=2-99.
DR PDBsum; 5DJB; -.
DR PDBsum; 5V74; -.
DR PDBsum; 6MZU; -.
DR PDBsum; 6MZV; -.
DR PDBsum; 6MZX; -.
DR PDBsum; 6MZY; -.
DR PDBsum; 6N06; -.
DR PDBsum; 6N07; -.
DR PDBsum; 6N09; -.
DR PDBsum; 6N0F; -.
DR PDBsum; 6N0G; -.
DR PDBsum; 6NER; -.
DR PDBsum; 6NLU; -.
DR AlphaFoldDB; D0LID5; -.
DR SMR; D0LID5; -.
DR IntAct; D0LID5; 4.
DR STRING; 502025.Hoch_5815; -.
DR EnsemblBacteria; ACY18291; ACY18291; Hoch_5815.
DR KEGG; hoh:Hoch_5815; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_064903_5_3_7; -.
DR OMA; QFREGVN; -.
DR OrthoDB; 1802372at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
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..99
FT /note="Bacterial microcompartment protein homohexamer"
FT /id="PRO_0000452545"
FT DOMAIN 4..88
FT /note="BMC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT MUTAGEN 28
FT /note="K->A: Forms larger hexamer patches, increases
FT hexamer stacking."
FT /evidence="ECO:0000269|PubMed:26617073"
FT MUTAGEN 78
FT /note="R->A: Forms smaller hexamer patches."
FT /evidence="ECO:0000269|PubMed:26617073"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:6NLU"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:6NLU"
FT STRAND 27..38
FT /evidence="ECO:0007829|PDB:6NLU"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:6NLU"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:6NLU"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:5DJB"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:5DJB"
SQ SEQUENCE 99 AA; 10114 MW; 419ED2546F2FB97F CRC64;
MADALGMIEV RGFVGMVEAA DAMVKAAKVE LIGYEKTGGG YVTAVVRGDV AAVKAATEAG
QRAAERVGEV VAVHVIPRPH VNVDAALPLG RTPGMDKSA
