ID A9CZ09_9GAMM Unreviewed; 316 AA.
AC A9CZ09;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Na(+)-translocating NADH-quinone reductase subunit F {ECO:0000313|EMBL:EDQ02226.1};
GN ORFNames=KT99_12689 {ECO:0000313|EMBL:EDQ02226.1};
OS Shewanella benthica KT99.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=314608 {ECO:0000313|EMBL:EDQ02226.1, ECO:0000313|Proteomes:UP000005839};
RN [1] {ECO:0000313|EMBL:EDQ02226.1, ECO:0000313|Proteomes:UP000005839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT99 {ECO:0000313|EMBL:EDQ02226.1,
RC ECO:0000313|Proteomes:UP000005839};
RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004533}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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:EDQ02226.1}.
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DR EMBL; ABIC01000004; EDQ02226.1; -; Genomic_DNA.
DR RefSeq; WP_005496657.1; NZ_ABIC01000004.1.
DR AlphaFoldDB; A9CZ09; -.
DR STRING; 314608.KT99_12689; -.
DR Proteomes; UP000005839; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43644; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR43644:SF1; NAD(P)H-FLAVIN REDUCTASE; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT DOMAIN 1..85
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 80..215
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 294..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 34514 MW; F1B50243965EA579 CRC64;
MSSHENLLDS LINHDIALPS TCGGGGTCGR CKIKVESKVN MTSADKSQLT EQELQAGYRL
ACQHNSDELK QLTLVDVTMA ASHELRLISS VFLSPYIKEL RFKSVSGERL EFKAGAFMRF
FIPAAQASSI PVDLPADLLH HWQEVLHMDY EHLACSRNYS LANGDAQTDE LVFTVKMQTS
PNQKVKPGIG SSYICNLAPG KTIEAVGPFE EFFAIESAKT DPTSPMVLIG AGSGMAPLKA
LIEEQLIKFN SSRPIHFYFG ARTQADLIYR DAFRQLAATF PNFKYIPVLS RVTSTEGNSG
DGAKICTGSS GRGSEH
//
