ID   NDH_STAS1               Reviewed;         402 AA.
AC   Q49W80;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Type II NADH:quinone oxidoreductase {ECO:0000250|UniProtKB:Q2FZV7};
DE            EC=1.6.5.9 {ECO:0000250|UniProtKB:Q2FZV7};
DE   AltName: Full=NDH-2 {ECO:0000250|UniProtKB:Q2FZV7};
GN   OrderedLocusNames=SSP1834;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC   -!- FUNCTION: Alternative, nonproton pumping NADH:quinone oxidoreductase
CC       that delivers electrons to the respiratory chain by oxidation of NADH
CC       and reduction of quinones, and contributes to the regeneration of
CC       NAD(+). {ECO:0000250|UniProtKB:Q2FZV7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC         Evidence={ECO:0000250|UniProtKB:Q2FZV7};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q2FZV7};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q2FZV7};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2FZV7}.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AP008934; BAE18979.1; -; Genomic_DNA.
DR   RefSeq; WP_011303523.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49W80; -.
DR   SMR; Q49W80; -.
DR   STRING; 342451.SSP1834; -.
DR   EnsemblBacteria; BAE18979; BAE18979; SSP1834.
DR   KEGG; ssp:SSP1834; -.
DR   PATRIC; fig|342451.11.peg.1830; -.
DR   eggNOG; COG1252; Bacteria.
DR   HOGENOM; CLU_021377_7_2_9; -.
DR   OMA; DHCIFLD; -.
DR   OrthoDB; 403436at2; -.
DR   Proteomes; UP000006371; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   3: Inferred from homology;
KW   Cell membrane; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..402
FT                   /note="Type II NADH:quinone oxidoreductase"
FT                   /id="PRO_0000287376"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         12..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         39..40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         83
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         302
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         319..320
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         379
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
SQ   SEQUENCE   402 AA;  44227 MW;  8F517A6F4CD9ED38 CRC64;
     MAQDRKKVLV LGAGYAGLQT ITKLQKQISA DEAEVTLINK NDYHYEATWL HEASAGTISY
     EDLLYPVESV VNKDKVNFVK AEVTKIDRNA KKVETDAGIF DFDILVVSLG FESETFGIKG
     MKDYAFQIEN VLTARKLSRH IEDKFANYAS SKQKDDKDLA IIVGGAGFTG VEFLGELTDR
     IPELCNKYGV EQSKVKITCV EAAPKMLPMF SDELVNHAVN YLENKGVEFK IGTPIVAANE
     KGFVVKVNDE EQQLEANTVV WAAGVRGSKL MEESFEGVKR GRIVTKQDLT IEGYDDIFVI
     GDCSAFIPAG EERPLPTTAQ IATQQGEHTA KNVKNILEGQ PTNEFEYVDR GTVCSLGAHD
     GVGVVYGRDI QGKKAAFMKK VIDTRAVFKL GGIGLAFKKG KF