ENCAP_MYCTU
ID ENCAP_MYCTU Reviewed; 265 AA.
AC I6WZG6; O07812;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Type 1 encapsulin shell protein {ECO:0000303|PubMed:24855650};
DE AltName: Full=Culture filtrate protein 29 {ECO:0000303|PubMed:9596740};
DE Short=CFP29 {ECO:0000303|PubMed:9596740};
DE Contains:
DE RecName: Full=Type 1 encapsulin shell protein, N-terminally processed;
GN Name=enc {ECO:0000303|PubMed:24855650};
GN Synonyms=cfp29 {ECO:0000303|PubMed:9596740}; OrderedLocusNames=Rv0798c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=9596740; DOI=10.1128/iai.66.6.2728-2735.1998;
RA Rosenkrands I., Rasmussen P.B., Carnio M., Jacobsen S., Theisen M.,
RA Andersen P.;
RT "Identification and characterization of a 29-kilodalton protein from
RT Mycobacterium tuberculosis culture filtrate recognized by mouse memory
RT effector cells.";
RL Infect. Immun. 66:2728-2735(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=20662102; DOI=10.1002/pmic.200900840;
RA Giri P.K., Kruh N.A., Dobos K.M., Schorey J.S.;
RT "Proteomic analysis identifies highly antigenic proteins in exosomes from
RT M. tuberculosis-infected and culture filtrate protein-treated
RT macrophages.";
RL Proteomics 10:3190-3202(2010).
RN [4] {ECO:0007744|PubMed:21969609}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=24855650; DOI=10.1074/jbc.m114.570119;
RA Contreras H., Joens M.S., McMath L.M., Le V.P., Tullius M.V., Kimmey J.M.,
RA Bionghi N., Horwitz M.A., Fitzpatrick J.A., Goulding C.W.;
RT "Characterization of a Mycobacterium tuberculosis nanocompartment and its
RT potential cargo proteins.";
RL J. Biol. Chem. 289:18279-18289(2014).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=34751132; DOI=10.7554/elife.74358;
RA Lien K.A., Dinshaw K., Nichols R.J., Cassidy-Amstutz C., Knight M.,
RA Singh R., Eltis L.D., Savage D.F., Stanley S.A.;
RT "A nanocompartment system contributes to defense against oxidative stress
RT in Mycobacterium tuberculosis.";
RL Elife 10:0-0(2021).
RN [7]
RP CLASSIFICATION.
RX PubMed=34362927; DOI=10.1038/s41467-021-25071-y;
RA Andreas M.P., Giessen T.W.;
RT "Large-scale computational discovery and analysis of virus-derived
RT microbial nanocompartments.";
RL Nat. Commun. 12:4748-4748(2021).
CC -!- FUNCTION: Shell component of a type 1 encapsulin nanocompartment in
CC situ; its cargo protects against oxidative stress at low pH. In situ
CC and in E.coli assembles into proteinaceous shells about 22 nm in
CC diameter with 2.5 nm thick walls (PubMed:34751132, PubMed:24855650).
CC Cargo proteins are targeted to the interior via their C-terminal
CC extensions; empty intact shells can be isolated in E.coli in the
CC absence of cargo protein. There are at least 4 possible cargo proteins,
CC DyP (encoded in the same locus), FolB, BfrB and Rv1762c; DyP and
CC Rv1762c have been identified in vivo (PubMed:24855650). Probably
CC involved in protection against oxidative damage from the host immune
CC response (Probable) (PubMed:34751132). A T-cell antigen found in
CC bacterial culture cell filtrates, stimulates mouse immune response.
CC Does not have detectable bacteriocin activity (PubMed:9596740).
CC {ECO:0000269|PubMed:24855650, ECO:0000269|PubMed:34751132,
CC ECO:0000269|PubMed:9596740, ECO:0000305|PubMed:24855650}.
CC -!- SUBUNIT: Multimeric (PubMed:9596740). The encapsulin nanocompartment is
CC formed by 60 subunits (Probable). Monomers form pentamers which
CC assemble to form shells. There are 12 pores where the pentamers meet as
CC well as 3-fold axis channels and dimer channels; none are larger than
CC 3-4 Angstroms in diameter. The N-terminus of the protein is inside the
CC shell, the C-terminus is outside (Probable).
CC {ECO:0000269|PubMed:9596740, ECO:0000305|PubMed:24855650}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:24855650}. Secreted {ECO:0000269|PubMed:9596740}.
CC Cell membrane {ECO:0000269|PubMed:9596740}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9596740}. Note=Encapsulin microcompartments of this
CC protein encapsulating DyP are found in situ (PubMed:34751132). Detected
CC at low levels in short-term culture filtrate, the nanocompartment is
CC very stable and may survive cell lysis, explaining its apparent
CC secretion (PubMed:9596740) (Probable). Detected in infected host (mouse
CC J774 cell line) exosomes (PubMed:20662102).
CC {ECO:0000269|PubMed:20662102, ECO:0000269|PubMed:34751132,
CC ECO:0000269|PubMed:9596740, ECO:0000305|PubMed:34751132}.
CC -!- PTM: The initiator methionine is partially removed. When isolated from
CC culture filtrate isoelectric focusing gives 3 bands, none of which are
CC glycosylated. {ECO:0000269|PubMed:9596740}.
CC -!- DISRUPTION PHENOTYPE: A single enc deletion survives less well after 3
CC days in 2.5 mM H2O2, pH 4.5 (mimics growth in the phagolysosome). A
CC double dyp-enc deletion mutant cannot produce encapsulin
CC nanocompartments, cells are highly sensitive to H2O2 at pH 4.5, mutants
CC exhibit significant dysregulation of redox homeostasis, survive less
CC well in C57BL/6 mouse-derived bone marrow cells and are more sensitive
CC to pyrazinamide treatment in infected BALB/C mice.
CC {ECO:0000269|PubMed:34751132}.
CC -!- MISCELLANEOUS: Stimulates a strong IFN-gamma response in memory immune
CC C57BL/6J mouse spleen T cells, recognized by monoclonal antibody HYB
CC 71-2. {ECO:0000269|PubMed:9596740}.
CC -!- SIMILARITY: Belongs to the encapsulin family. Family 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; Y12820; CAA73350.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43546.1; -; Genomic_DNA.
DR RefSeq; NP_215313.1; NC_000962.3.
DR RefSeq; WP_003404092.1; NZ_NVQJ01000064.1.
DR AlphaFoldDB; I6WZG6; -.
DR SMR; I6WZG6; -.
DR STRING; 83332.Rv0798c; -.
DR MEROPS; U56.001; -.
DR PaxDb; I6WZG6; -.
DR PRIDE; I6WZG6; -.
DR DNASU; 885460; -.
DR GeneID; 885460; -.
DR KEGG; mtu:Rv0798c; -.
DR PATRIC; fig|83332.111.peg.885; -.
DR TubercuList; Rv0798c; -.
DR eggNOG; COG1659; Bacteria.
DR OMA; DSDWQPV; -.
DR PhylomeDB; I6WZG6; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR007544; Linocin_M18.
DR Pfam; PF04454; Linocin_M18; 1.
DR PIRSF; PIRSF019254; CFP29; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Encapsulin nanocompartment;
KW Membrane; Reference proteome; Secreted; Virulence.
FT CHAIN 1..265
FT /note="Type 1 encapsulin shell protein"
FT /id="PRO_0000455313"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:9596740"
FT CHAIN 2..265
FT /note="Type 1 encapsulin shell protein, N-terminally
FT processed"
FT /id="PRO_0000455314"
FT CONFLICT 242
FT /note="V -> E (in Ref. 1; CAA73350)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 28830 MW; 00E7E96904D3B33A CRC64;
MNNLYRDLAP VTEAAWAEIE LEAARTFKRH IAGRRVVDVS DPGGPVTAAV STGRLIDVKA
PTNGVIAHLR ASKPLVRLRV PFTLSRNEID DVERGSKDSD WEPVKEAAKK LAFVEDRTIF
EGYSAASIEG IRSASSNPAL TLPEDPREIP DVISQALSEL RLAGVDGPYS VLLSADVYTK
VSETSDHGYP IREHLNRLVD GDIIWAPAID GAFVLTTRGG DFDLQLGTDV AIGYASHDTD
TVRLYLQETL TFLCYTAEAS VALSH
