ENCAP_KUEST
ID ENCAP_KUEST Reviewed; 363 AA.
AC Q1Q6L7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Diheme-cytochrome-encapsulin shell fusion protein;
DE AltName: Full=Type 1 encapsulin shell protein;
DE Flags: Precursor;
GN Name=enc {ECO:0000305}; ORFNames=kuste2478;
OS Kuenenia stuttgartiensis.
OC Bacteria; Planctomycetes; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Candidatus Kuenenia.
OX NCBI_TaxID=174633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUST_E;
RX PubMed=16598256; DOI=10.1038/nature04647;
RA Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., Taylor M.W.,
RA Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N.,
RA Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A.,
RA Snel B., Dutilh B.E., Op den Camp H.J., van der Drift C., Cirpus I.,
RA van de Pas-Schoonen K.T., Harhangi H.R., van Niftrik L., Schmid M.,
RA Keltjens J., van de Vossenberg J., Kartal B., Meier H., Frishman D.,
RA Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M.,
RA Le Paslier D.;
RT "Deciphering the evolution and metabolism of an anammox bacterium from a
RT community genome.";
RL Nature 440:790-794(2006).
RN [2]
RP FUNCTION, PROBABLE COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=28263314; DOI=10.1038/nmicrobiol.2017.29;
RA Giessen T.W., Silver P.A.;
RT "Widespread distribution of encapsulin nanocompartments reveals functional
RT diversity.";
RL Nat. Microbiol. 2:17029-17029(2017).
RN [3]
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: Fusion of the shell and cargo protein of a type 1 encapsulin
CC nanocompartment. Protein missing its signal peptide makes 33 nm
CC particles in E.coli (called cEnc), protein missing its signal peptide
CC and diheme domain (residues 1-86, called Enc) makes 29 nm particles.
CC The cEnc nancompartment encloses c-type heme. The cargo protein NIR-HAO
CC (AC P0DV45) is probably targeted to the nanocompartment by its
CC association with the diheme domain in cEnc; removal of the diheme
CC domain in Enc halves the amount of cargo.
CC {ECO:0000305|PubMed:28263314}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:28263314};
CC Note=Binds 2 heme groups per molecule. {ECO:0000305|PubMed:28263314};
CC -!- SUBUNIT: The encapsulin nanocompartment is probably formed by 180
CC monomers, with the N-terminus (diheme domain) inside (Probable). There
CC are 36 pores where the pentamers meet as well as 3-fold axis channels
CC and dimer channels (By similarity). {ECO:0000250|UniProtKB:Q1D6H4,
CC ECO:0000305|PubMed:28263314}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:28263314}. Note=This type 1 encapsulin
CC nanocompartment may be targeted to the anammoxosome. {ECO:0000305}.
CC -!- MISCELLANEOUS: In (PubMed:28263314) the signal peptide was removed
CC prior to generating the constructs for expression in E.coli.
CC {ECO:0000269|PubMed:28263314}.
CC -!- SIMILARITY: Belongs to the encapsulin family. Family 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CT573071; CAJ73225.1; -; Genomic_DNA.
DR SMR; Q1Q6L7; -.
DR GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR007544; Linocin_M18.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF04454; Linocin_M18; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
PE 1: Evidence at protein level;
KW Encapsulin nanocompartment; Heme; Iron; Metal-binding; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..363
FT /note="Diheme-cytochrome-encapsulin shell fusion protein"
FT /evidence="ECO:0000255"
FT /id="PRO_5004195658"
FT REGION 37..74
FT /note="Diheme c-type cytochrome"
FT /evidence="ECO:0000305|PubMed:28263314"
FT REGION 75..94
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:28263314"
FT REGION 95..363
FT /note="Encapsulin domain"
FT /evidence="ECO:0000305|PubMed:28263314"
FT BINDING 44
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:28263314"
FT BINDING 47
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:28263314"
FT BINDING 48
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:28263314"
FT BINDING 67
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:28263314"
FT BINDING 70
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:28263314"
FT BINDING 71
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:28263314"
SQ SEQUENCE 363 AA; 40021 MW; 3A667BB5A6A63AB3 CRC64;
MVMGILNTFK KVYAVTGFFA LLAVFSLSQV GSSAFAACAK VDDCFSCHTT QELNAVHKNT
PYQGQSCIVC HKAFAADDTC SDAKDGRFAK ISSEININKE DWNKIQRAVH ETTEKHLVGR
KFLNIYGPLG TGAQSVPLDT YGLPSWASID MLGEGNEAIH PLKREIAQIY LIYKDFWLFR
RDIEFSKKCE TPIDISAAIG AAVSVSRKED DMVFNGLSEM GIPGLLTASG RNIMKLSDWS
VIGNGFQDVV LAVEKLTSRG FNGPFALVVS PKLYAYLHRV YERTGQLEIQ GVKELVNGGV
YQSYVFNKDV ALVIATGSLN MDLAVGSNYK VEYWGPQDLN HRFRVVGSSV LRIKCPQAIC
TLE
