ENCP2_SYNE7
ID ENCP2_SYNE7 Reviewed; 306 AA.
AC Q55032; Q7BA86;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Type 2A encapsulin shell protein SrpI {ECO:0000303|PubMed:33821786};
GN Name=enc {ECO:0000305}; Synonyms=sprI {ECO:0000303|PubMed:7603442};
GN OrderedLocusNames=Synpcc7942_B2662; ORFNames=pANL38;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OG Plasmid 1, and Plasmid pANL.
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RX PubMed=7603442; DOI=10.1007/bf00290354;
RA Nicholson M.L., Gaasenbeek M., Laudenbach D.E.;
RT "Two enzymes together capable of cysteine biosynthesis are encoded on a
RT cyanobacterial plasmid.";
RL Mol. Gen. Genet. 247:623-632(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RA Holtman C.K., Chen Y., Sandoval P., Socias T., Mohler B.J., Youderian P.,
RA Golden S.S.;
RT "pANL, the large plasmid of Synechococcus elongatus PCC 7942.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of plasmid 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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).
RN [5] {ECO:0007744|PDB:6X8M, ECO:0007744|PDB:6X8T}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.20 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, INDUCTION BY SULFUR STARVATION, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RX PubMed=33821786; DOI=10.7554/elife.59288;
RA Nichols R.J., LaFrance B., Phillips N.R., Radford D.R., Oltrogge L.M.,
RA Valentin-Alvarado L.E., Bischoff A.J., Nogales E., Savage D.F.;
RT "Discovery and characterization of a novel family of prokaryotic
RT nanocompartments involved in sulfur metabolism.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Shell component of a type 2A encapsulin nanocompartment.
CC Expression in E.coli generates nanocompartments with an average
CC diameter of 25 nm. They can be disassembled by treatment with 6M
CC guanidine hydrochloride and reassembled with cargo. The nanocompartment
CC is probably involved in sulfur metabolism (PubMed:33821786). Probably
CC allows passage of cysteine into its interior; during growth in light
CC the physiological pH is 8-8.4, about 30-54% of free cysteine (charge
CC -1) would be able to pass through the shell (Probable).
CC {ECO:0000269|PubMed:33821786, ECO:0000305|PubMed:33821786}.
CC -!- SUBUNIT: The 24.5 nm encapsulin nanocompartment is formed by 60
CC subunits; monomers form pentamers which assemble to form shells. There
CC are 12 positively charged pores where the pentamers meet with a minimal
CC pore diameter of 3.7 Angstroms as well 3-fold axis channels and dimer
CC channels. {ECO:0000269|PubMed:33821786}.
CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC {ECO:0000269|PubMed:33821786}. Note=Unlike type 1 subfamily
CC encapsulins, the nanocompartment has a raised protuberance around the
CC 5-fold pores. {ECO:0000269|PubMed:33821786}.
CC -!- INDUCTION: Transcriptionally induced in the absence of sulfur, requires
CC CysR for transcription. Part of the srpG-srpH-srpI operon
CC (PubMed:7603442). Present in when grown in sulfur-containing media,
CC induced 7-fold after 48 hours of sulfur starvation (at protein level)
CC (PubMed:33821786). {ECO:0000269|PubMed:33821786,
CC ECO:0000269|PubMed:7603442}.
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:0000269|PubMed:33821786}.
CC -!- DISRUPTION PHENOTYPE: No growth phenotype of a single sprI or double
CC srpI-cyd deletion mutant in the presence or absence of sulfur.
CC {ECO:0000269|PubMed:33821786}.
CC -!- SIMILARITY: Belongs to the encapsulin family. Family 2A subfamily.
CC {ECO:0000305|PubMed:33821786}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U23436; AAA86727.1; -; Genomic_DNA.
DR EMBL; AF441790; AAM81164.1; -; Genomic_DNA.
DR EMBL; CP000101; ABB58691.1; -; Genomic_DNA.
DR RefSeq; NP_665777.1; NC_004073.2.
DR RefSeq; WP_011055154.1; NC_007595.1.
DR PDB; 6X8M; EM; 2.20 A; A=1-306.
DR PDB; 6X8T; EM; 2.90 A; A=1-306.
DR PDBsum; 6X8M; -.
DR PDBsum; 6X8T; -.
DR AlphaFoldDB; Q55032; -.
DR SMR; Q55032; -.
DR STRING; 1140.Synpcc7942_B2662; -.
DR PRIDE; Q55032; -.
DR EnsemblBacteria; ABB58691; ABB58691; Synpcc7942_B2662.
DR KEGG; syf:Synpcc7942_B2662; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_089302_0_0_3; -.
DR OMA; WLVHLLQ; -.
DR OrthoDB; 250058at2; -.
DR BioCyc; SYNEL:SYNPCC7942_B2662-MON; -.
DR GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR InterPro; IPR045641; MmpI-like_C.
DR Pfam; PF19307; PCLP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Encapsulin nanocompartment; Plasmid.
FT CHAIN 1..306
FT /note="Type 2A encapsulin shell protein SrpI"
FT /id="PRO_0000072194"
FT SITE 192
FT /note="5-fold pore central residue"
FT /evidence="ECO:0000269|PubMed:33821786"
FT SITE 194
FT /note="5-fold pore central residue"
FT /evidence="ECO:0000269|PubMed:33821786"
FT SITE 196
FT /note="5-fold pore central residue"
FT /evidence="ECO:0000269|PubMed:33821786"
FT SITE 262
FT /note="May bind cargo"
FT /evidence="ECO:0000305|PubMed:33821786"
FT SITE 273
FT /note="May bind cargo"
FT /evidence="ECO:0000305|PubMed:33821786"
FT SITE 304
FT /note="5-fold pore central residue"
FT /evidence="ECO:0000269|PubMed:33821786"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:6X8M"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6X8M"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:6X8M"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6X8M"
FT HELIX 112..134
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6X8M"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6X8M"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:6X8M"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6X8T"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:6X8M"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 269..285
FT /evidence="ECO:0007829|PDB:6X8M"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:6X8M"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:6X8M"
SQ SEQUENCE 306 AA; 34360 MW; 6746AE7222A16B04 CRC64;
MTDNAPQLAL RDVAARQLAN ATKTVPQLRT ITPRWLVRLL HWTPVEAGIY RVNQVKDASQ
ITVACSERDE SELPETFVDY IDNPREYLLS AVNTVVDVHT RISDLYSNPH DQIREQLRLT
IEIMKERQES ELINSREYGL LNNVAPGQLV HTRNGAPTPD DLDELLIRVW KEPAFFLAHP
QAIAAFGREC TRRGVPPATV SLFGSSFITW RGVPLIPSDK VPLENGKTKI LLLRVGESRQ
GVVGLYQPNL PGEQGMGLSV RFMGINRKAL ASYLVSLYCS LAVLTDDALA VLDNVDVTQY
HTYRYN
