ID A0A0U5NL46_9CLOT Unreviewed; 240 AA.
AC A0A0U5NL46;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU368020};
GN ORFNames=BN3456_00530 {ECO:0000313|EMBL:CUX21878.1};
OS Clostridium sp. C105KSO13.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1776045 {ECO:0000313|EMBL:CUX21878.1, ECO:0000313|Proteomes:UP000198973};
RN [1] {ECO:0000313|EMBL:CUX21878.1, ECO:0000313|Proteomes:UP000198973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C105KSO131 {ECO:0000313|EMBL:CUX21878.1};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC {ECO:0000256|RuleBase:RU368020}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the UPF0718 family.
CC {ECO:0000256|ARBA:ARBA00006386}.
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DR EMBL; FBWL01000148; CUX21878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5NL46; -.
DR STRING; 1776045.BN3456_00530; -.
DR OrthoDB; 9798408at2; -.
DR Proteomes; UP000198973; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR001080; 3Fe4S_ferredoxin.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR005524; DUF318.
DR Pfam; PF03773; ArsP_1; 1.
DR Pfam; PF13370; Fer4_13; 1.
DR PRINTS; PR00352; 3FE4SFRDOXIN.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|RuleBase:RU368020};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU368020};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU368020};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368020};
KW Reference proteome {ECO:0000313|Proteomes:UP000198973};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU368020}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..205
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 240 AA; 26845 MW; 7FABEFA8460A6E72 CRC64;
MTIIKKIKEN LFLVIVVLAY IIMFIAKPAM GIESVKSSGY YIKEMLMIMP VIFVLTALLD
MWVSKEKITQ YLGKDAKAKG VLFSFVVGSI SAGPVYAAFP MCVMLHKKGA SIRNIVIILS
SWAVIKIPML INEAKFLGPK FMAVRWVLTI IAIIIFSWIT AKIIKDKDLP GEVLTQAGLH
INRDACMGCT LCAKNYPGVF EMENKRALVR PHEALDMEKL ENAIKACPVK AITYNEDRKN
//
