ENCP2_MYCLE
ID ENCP2_MYCLE Reviewed; 307 AA.
AC P46841; O32976;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Type 2A encapsulin shell protein {ECO:0000250|UniProtKB:Q55032};
DE AltName: Full=35 kDa antigen {ECO:0000303|PubMed:7476185};
DE AltName: Full=Major membrane protein I {ECO:0000303|PubMed:7476185};
DE Short=MMPI {ECO:0000303|PubMed:7476185};
GN Name=enc {ECO:0000305}; Synonyms=mmpI {ECO:0000303|PubMed:7476185};
GN OrderedLocusNames=ML0841; ORFNames=MLCB22.45c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-68; 71-93;
RP 122-130; 145-170; 176-194; 198-210; 215-221; 243-262 AND 282-306,
RP ANTIGENICITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=Armadillo isolate;
RX PubMed=7476185; DOI=10.1111/j.1365-2958.1995.tb02314.x;
RA Winter N., Triccas J.A., Rivoire B., Pessolani M.C.V., Eiglmeier K.,
RA Lim E.-M., Hunter S.W., Brennan P.J., Britton W.J.;
RT "Characterization of the gene encoding the immunodominant 35 kDa protein of
RT Mycobacterium leprae.";
RL Mol. Microbiol. 16:865-876(1995).
RN [2]
RP ANTIGENICITY, AND SUBUNIT.
RX PubMed=8945562; DOI=10.1128/iai.64.12.5171-5177.1996;
RA Triccas J.A., Roche P.W., Winter N., Feng C.G., Butlin C.R., Britton W.J.;
RT "A 35-kilodalton protein is a major target of the human immune response to
RT Mycobacterium leprae.";
RL Infect. Immun. 64:5171-5177(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
RN [4]
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 2A encapsulin nanocompartment.
CC Forms encapsulin nanocompartments about 24 nm in diameter from 60
CC monomers. Probably encapsulates at least cysteine desulfurase (CyD, AC
CC O32975) and allows passage of cysteine into its interior, probably
CC involved in sulfur metabolism (By similarity). Expression in
CC M.smegmatis generates a multimeric protein, whereas expression in
CC E.coli does not (PubMed:8945562). {ECO:0000250|UniProtKB:Q55032,
CC ECO:0000269|PubMed:8945562}.
CC -!- SUBUNIT: Homooligomeric (PubMed:7476185, PubMed:8945562). The
CC encapsulin nanocompartment is formed by 60 subunits; monomers form
CC pentamers which assemble to form shells. There are 12 charged pores
CC where the pentamers meet as well as 3-fold axis channels and dimer
CC channels (By similarity). {ECO:0000250|UniProtKB:Q55032,
CC ECO:0000269|PubMed:7476185, ECO:0000269|PubMed:8945562}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000250|UniProtKB:Q55032}. Cytoplasm, cytosol
CC {ECO:0000305|PubMed:7476185}. Cell membrane
CC {ECO:0000305|PubMed:7476185}; Peripheral membrane protein
CC {ECO:0000305|PubMed:7476185}. Note=Soluble or peripheral membrane
CC protein. {ECO:0000305|PubMed:7476185}.
CC -!- DOMAIN: Has 4 domains; an N-terminal arm not found in the type 1
CC subfamily, a discontinuous peripheral domain (P), an elongated loop (E)
CC and the discontinuous axial domain (A). {ECO:0000250|UniProtKB:Q55032}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7476185}.
CC -!- MISCELLANEOUS: Dominant antigen for this bacteria, could possibly be
CC used in vaccine formulation and/or for diagnosis (PubMed:7476185,
CC PubMed:8945562). Protein expressed in M.smegmatis stimulates a gamma
CC interferon-secreting T-cell proliferative response (PubMed:8945562).
CC {ECO:0000269|PubMed:7476185, ECO:0000269|PubMed:8945562}.
CC -!- SIMILARITY: Belongs to the encapsulin family. Family 2A subfamily.
CC {ECO:0000305}.
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DR EMBL; U15651; AAB60193.1; -; Genomic_DNA.
DR EMBL; Z98741; CAB11410.1; -; Genomic_DNA.
DR EMBL; AL583919; CAC30351.1; -; Genomic_DNA.
DR PIR; S77651; S77651.
DR PIR; T44910; T44910.
DR RefSeq; NP_301635.1; NC_002677.1.
DR RefSeq; WP_010907959.1; NC_002677.1.
DR AlphaFoldDB; P46841; -.
DR SMR; P46841; -.
DR STRING; 272631.ML0841; -.
DR EnsemblBacteria; CAC30351; CAC30351; CAC30351.
DR KEGG; mle:ML0841; -.
DR PATRIC; fig|272631.5.peg.1556; -.
DR Leproma; ML0841; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_089302_0_0_11; -.
DR OMA; WLVHLLQ; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0140737; C:encapsulin nanocompartment; IC:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR045641; MmpI-like_C.
DR Pfam; PF19307; PCLP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Direct protein sequencing;
KW Encapsulin nanocompartment; Membrane; Reference proteome.
FT CHAIN 1..307
FT /note="Type 2A encapsulin shell protein"
FT /id="PRO_0000096512"
FT CONFLICT 55
FT /note="R -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62..68
FT /note="VAVKAEA -> RRSVSQQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..88
FT /note="SPR -> P (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="K -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..154
FT /note="IR -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..164
FT /note="DD -> PT (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="L -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..193
FT /note="FGREA -> AQRNN (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="S -> VQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="G -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="R -> L (in Ref. 1; AAB60193)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..262
FT /note="LS -> DIQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="I -> T (in Ref. 1; AAB60193)"
FT /evidence="ECO:0000305"
FT CONFLICT 272..274
FT /note="AIA -> SDR (in Ref. 1; AAB60193)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="T -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="A -> V (in Ref. 1; AAB60193)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="D -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="D -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="E -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 33651 MW; F31F59C2AF432428 CRC64;
MTSAQNESQA LGDLAAGQLA NATKTVPQLS TITPRWLLHL LNWVPVEAGV YRVNRVVNPE
RVAVKAEAGA GTEAPLPETF VDYETSPREY TLRTISTLLD IHTRVSDLYS SPHDQITQQL
RLTIETIKER QECELVNSPE FGLLAQVTPE QTIRTFAGAP TPDDLDALIT KVWKMPSFFL
THPQGIAAFG REATYRGVPP VVVSLFGAQF ITWRGIPLIP SDKVPVQDGE TKFILVRTGE
ERQGVVGLFQ PGLVGEQAPG LSVRFTGINQ AAIATYLVTL YTSLAVLTDD ALAVLDNVAV
DQFHEYK
