ID   FER_QUATH               Reviewed;         122 AA.
AC   A0A0F5HNC1; A0A0F5ICV7;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Ferredoxin {ECO:0000303|PubMed:28263314};
DE   AltName: Full=Fer cargo protein {ECO:0000303|PubMed:28263314};
GN   Name=fer {ECO:0000303|PubMed:28263314};
GN   ORFNames=QY95_01591 {ECO:0000312|EMBL:KKB43346.1};
OS   Quasibacillus thermotolerans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Quasibacillus.
OX   NCBI_TaxID=1221996;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTCC 10057 / 5.5LF 38TD, and MTCC 8252;
RX   PubMed=28947104; DOI=10.1016/j.syapm.2017.07.010;
RA   Verma A., Pal Y., Khatri I., Ojha A.K., Gruber-Vodicka H., Schumann P.,
RA   Dastager S., Subramanian S., Mayilraj S., Krishnamurthi S.;
RT   "Examination into the taxonomic position of Bacillus thermotolerans Yang et
RT   al., 2013, proposal for its reclassification into a new genus and species
RT   Quasibacillus thermotolerans gen. nov., comb. nov. and reclassification of
RT   B. encimensis Dastager et al., 2015 as a later heterotypic synonym of B.
RT   badius.";
RL   Syst. Appl. Microbiol. 40:411-422(2017).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RC   STRAIN=MTCC 10057 / 5.5LF 38TD;
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).
CC   -!- FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. An
CC       iron-binding protein probably involved in iron mineralization in the
CC       encapsulin nanocompartment. 2 different cargo proteins have been
CC       identified (IMEF and Fer); when both are expressed in E.coli with the
CC       shell protein only IMEF is detected within the nanocompartment. E.coli
CC       expressing all 3 genes stores the largest amount of iron and is
CC       protected from Fe/H2O2-induced oxidative stress.
CC       {ECO:0000269|PubMed:28263314}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC       Note=Binds 1 2Fe-2S cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
CC   -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC       {ECO:0000269|PubMed:28263314}.
CC   -!- DOMAIN: The N-terminus (targeting peptide) is probably responsible for
CC       targeting to the encapsulin nanocompartment.
CC       {ECO:0000305|PubMed:28263314}.
CC   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; JWIR02000003; KKB43346.1; -; Genomic_DNA.
DR   RefSeq; WP_052717249.1; NZ_JWJE02000035.1.
DR   EnsemblBacteria; KKB43346; KKB43346; QY95_01591.
DR   OrthoDB; 1837979at2; -.
DR   Proteomes; UP000031563; Unassembled WGS sequence.
DR   GO; GO:0140737; C:encapsulin nanocompartment; IDA:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   Pfam; PF00111; Fer2; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Encapsulin nanocompartment; Iron; Iron storage; Iron-sulfur;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..122
FT                   /note="Ferredoxin"
FT                   /id="PRO_0000455330"
FT   DOMAIN          40..122
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          8..14
FT                   /note="Targeting peptide"
FT                   /evidence="ECO:0000305|PubMed:28263314"
FT   BINDING         75
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         80
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         83
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         117
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   122 AA;  13351 MW;  755C9C7E80800F5F CRC64;
     MSHDRRLTVG SLLPNQPRPV AVPKAPSVVQ PSKQPLPEKA IIRLEQNGRS FSVRHVKGNL
     LTEGLSQGLP LQYKCRKGTC GVCTVKVTDG ASRLSLPNQQ EHKKLQGNIK SGFRLACQAN
     ME