ID   BMCP_HALO1              Reviewed;          96 AA.
AC   D0LHE5;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Bacterial microcompartment shell vertex protein;
DE            Short=BMC-P {ECO:0000303|PubMed:28642439};
GN   OrderedLocusNames=Hoch_5814;
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] {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:6MZX, ECO:0007744|PDB:6MZY}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   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: Forms vertices in bacterial microcompartment (BMC) shells.
CC       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 BMC with a molecular mass of 6.5 MDa. There are 12 BMC-P
CC       pentamers per BMC. The shell facets are 20-30 Angstroms thick, with 1
CC       of BMC-T trimers protruding to the exterior.
CC       {ECO:0000269|PubMed:28642439, ECO:0000269|PubMed:30833088}.
CC   -!- SUBUNIT: Homopentamer. The base of the pyramid faces outward.
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   -!- DISRUPTION PHENOTYPE: Not essential for BMC formation; when an
CC       artificial operon without BMC-P proteins (Hoch_5815, Hoch_5812,
CC       Hoch_3341, Hoch_5816) is expressed in E.coli BMC shells are made.
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). {ECO:0000269|PubMed:24631000,
CC       ECO:0000269|PubMed:28642439, ECO:0000269|PubMed:31075444}.
CC   -!- MISCELLANEOUS: One of 3 BMC-P proteins in this bacteria, the others are
CC       Hoch_4425 and Hoch_4426. {ECO:0000269|PubMed:21304682}.
CC   -!- SIMILARITY: Belongs to the CcmL/EutN family. {ECO:0000305}.
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DR   EMBL; CP001804; ACY18290.1; -; Genomic_DNA.
DR   RefSeq; WP_012830882.1; NC_013440.1.
DR   PDB; 5V74; X-ray; 3.51 A; 11/21/31/41/A1/B1/C1/D1/E1/F1/G1/H1/I1/J1/K1/L1/M1/N1/O1/P1/Q1/R1/S1/T1/U1/V1/W1/X1/Y1/Z1=1-96.
DR   PDB; 6MZX; EM; 3.00 A; A1=1-96.
DR   PDB; 6MZY; EM; 3.30 A; A1=1-96.
DR   PDBsum; 5V74; -.
DR   PDBsum; 6MZX; -.
DR   PDBsum; 6MZY; -.
DR   AlphaFoldDB; D0LHE5; -.
DR   SMR; D0LHE5; -.
DR   IntAct; D0LHE5; 1.
DR   STRING; 502025.Hoch_5814; -.
DR   EnsemblBacteria; ACY18290; ACY18290; Hoch_5814.
DR   KEGG; hoh:Hoch_5814; -.
DR   eggNOG; COG4576; Bacteria.
DR   HOGENOM; CLU_148498_0_1_7; -.
DR   OMA; GAGINEW; -.
DR   OrthoDB; 1832681at2; -.
DR   Proteomes; UP000001880; Chromosome.
DR   GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR   CDD; cd01614; EutN_CcmL; 1.
DR   Gene3D; 2.40.50.220; -; 1.
DR   InterPro; IPR004992; EutN_CcmL.
DR   InterPro; IPR036677; EutN_CcmL_sf.
DR   PANTHER; PTHR36539; PTHR36539; 1.
DR   Pfam; PF03319; EutN_CcmL; 1.
DR   SUPFAM; SSF159133; SSF159133; 1.
DR   PROSITE; PS51932; BMV; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacterial microcompartment; Reference proteome.
FT   CHAIN           1..96
FT                   /note="Bacterial microcompartment shell vertex protein"
FT                   /id="PRO_0000452549"
FT   DOMAIN          1..83
FT                   /note="BMV"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01280"
SQ   SEQUENCE   96 AA;  9856 MW;  1439E699FE11390E CRC64;
     MVLGKVVGTV VASRKEPRIE GLSLLLVRAC DPDGTPTGGA VVCADAVGAG VGEVVLYASG
     SSARQTEVTN NRPVDATIMA IVDLVEMGGD VRFRKD