ID F7NDM4_9FIRM Unreviewed; 662 AA.
AC F7NDM4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Putative iron-sulfur-binding reductase {ECO:0000313|EMBL:EGO65886.1};
GN ORFNames=ALO_00655 {ECO:0000313|EMBL:EGO65886.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO65886.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO65886.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO65886.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGO65886.1}.
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; AFGF01000007; EGO65886.1; -; Genomic_DNA.
DR RefSeq; WP_004573045.1; NZ_AFGF01000007.1.
DR AlphaFoldDB; F7NDM4; -.
DR STRING; 1009370.ALO_00655; -.
DR eggNOG; COG0247; Bacteria.
DR Proteomes; UP000003240; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 1.20.950.20; Transmembrane di-heme cytochromes, Chain C; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR036197; NarG-like_sf.
DR PANTHER; PTHR43255:SF6; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED; 1.
DR PANTHER; PTHR43255; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED-RELATED; 1.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF103501; Respiratory nitrate reductase 1 gamma chain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 271..298
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 333..365
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 662 AA; 73053 MW; CD9C1C891E8D45E2 CRC64;
MPASRPLGMY HDSYWIMYVL MLVAFAIFAK GVYDRYKLWK VGAPENFKPD MAGLIRLIKN
SFGHARLLRE PGPGVAHAVV FWAFAVCAVG TLSIAVTEDL GIPLFQGGYY LILSLAMDLL
GLGAVIGIGF AAYRRYVLQP AGLDNKPDDL YTLLLIEAIL VTGFLLEGLR MAAIPDPWAA
WSPVGAAVAA LFSGGSPAGL RSAHQAVWWI HLLFSFGFIA YIPYSKMFHM LSGSANIALA
QGNAAQKMKP IDMEDETVEQ FGVAELQQFT WKQLLDSDAC IRCGRCQDNC PAYQTGKPLS
PKKLVQDFKT HLNQKGPLLV KGATAEETSA SLVPDVVNEE EVWACTTCAA CEHQCPVYVE
HVPKIIDLRR NLTMMESAFP HEVKLTFTGM ERNGNPWNIS RSEAKWMSKE LGVASLAEKP
EVEYLFFPGC SGVFDERNKK VTTAVVKLLQ KAGVSFGVLG SEQTCCGDSA RRLGNEYLYQ
TLAQGNIEAL NEYGVKKIIT TCPHCFNTLK NEYPQFGGNY EVIHHVTFLA QLVKEGKLQP
QKSVDATCTY HDSCYLGRYN DIYQEPRALL ASIPGISSKE MEKSHEKSFC CGAGGGRMWL
EETIGERINV KRTEQALETG AGMIVSACPF CLTMMEDGTK LKSVDETVKT KDLAEVLWES
VQ
//
