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Database: UniProt
Entry: P33934
LinkDB: P33934
Original site: P33934 
ID   NAPH_ECOLI              Reviewed;         287 AA.
AC   P33934; Q2MAN9;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   10-APR-2019, entry version 144.
DE   RecName: Full=Ferredoxin-type protein NapH {ECO:0000305};
DE   AltName: Full=Ubiquinol--[NapC cytochrome c] reductase NapH subunit {ECO:0000305};
GN   Name=napH; Synonyms=yejZ; OrderedLocusNames=b2204, JW2192;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / BHB2600;
RA   Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA   Church G.M.;
RT   "Automated multiplex sequencing of the E.coli genome.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11967083;
RA   Brondijk T.H., Fiegen D., Richardson D.J., Cole J.A.;
RT   "Roles of NapF, NapG and NapH, subunits of the Escherichia coli
RT   periplasmic nitrate reductase, in ubiquinol oxidation.";
RL   Mol. Microbiol. 44:245-255(2002).
RN   [5]
RP   FUNCTION, INTERACTION WITH NAPC, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=14674886; DOI=10.1042/BJ20031115;
RA   Brondijk T.H., Nilavongse A., Filenko N., Richardson D.J., Cole J.A.;
RT   "NapGH components of the periplasmic nitrate reductase of Escherichia
RT   coli K-12: location, topology and physiological roles in quinol
RT   oxidation and redox balancing.";
RL   Biochem. J. 379:47-55(2004).
RN   [6]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
CC   -!- FUNCTION: Required for electron transfer from ubiquinol, via NapC,
CC       to the periplasmic nitrate reductase NapAB complex.
CC       {ECO:0000269|PubMed:11967083, ECO:0000269|PubMed:14674886}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC       Note=Binds 2 [4Fe-4S] cluster. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711};
CC   -!- SUBUNIT: Interacts with NapC. {ECO:0000269|PubMed:14674886}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:14674886, ECO:0000269|PubMed:15919996}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:14674886}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of both napG and napH genes has
CC       little effect on the overall rate of nitrate reduction during
CC       growth in the glycerol/nitrate medium. However, during growth in
CC       the glucose/nitrate medium, the double mutant shows a decreased
CC       rate of electron transfer that correlates with decreased NapAB
CC       activity. {ECO:0000269|PubMed:11967083}.
DR   EMBL; U00008; AAA16396.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75264.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76667.1; -; Genomic_DNA.
DR   PIR; B64990; B64990.
DR   RefSeq; NP_416708.1; NC_000913.3.
DR   RefSeq; WP_000013515.1; NZ_LN832404.1.
DR   ProteinModelPortal; P33934; -.
DR   BioGrid; 4262223; 14.
DR   DIP; DIP-10310N; -.
DR   IntAct; P33934; 2.
DR   STRING; 511145.b2204; -.
DR   TCDB; 3.D.11.1.1; the periplasmic nitrate reductase complex (nap) complex family.
DR   PaxDb; P33934; -.
DR   PRIDE; P33934; -.
DR   EnsemblBacteria; AAC75264; AAC75264; b2204.
DR   EnsemblBacteria; BAE76667; BAE76667; BAE76667.
DR   GeneID; 945984; -.
DR   KEGG; ecj:JW2192; -.
DR   KEGG; eco:b2204; -.
DR   PATRIC; fig|1411691.4.peg.32; -.
DR   EchoBASE; EB1992; -.
DR   EcoGene; EG12062; napH.
DR   eggNOG; ENOG4105GXZ; Bacteria.
DR   eggNOG; COG0348; LUCA.
DR   HOGENOM; HOG000275510; -.
DR   InParanoid; P33934; -.
DR   KO; K02574; -.
DR   PhylomeDB; P33934; -.
DR   BioCyc; EcoCyc:NAPH-MONOMER; -.
DR   BioCyc; ECOL316407:JW2192-MONOMER; -.
DR   BioCyc; MetaCyc:NAPH-MONOMER; -.
DR   PRO; PR:P33934; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011886; NapH_MauN.
DR   Pfam; PF13237; Fer4_10; 1.
DR   Pfam; PF12801; Fer4_5; 2.
DR   TIGRFAMs; TIGR02163; napH_; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    287       Ferredoxin-type protein NapH.
FT                                /FTId=PRO_0000159283.
FT   TOPO_DOM      1     29       Cytoplasmic.
FT                                {ECO:0000269|PubMed:14674886}.
FT   TRANSMEM     30     50       Helical. {ECO:0000255}.
FT   TOPO_DOM     51     79       Periplasmic.
FT                                {ECO:0000269|PubMed:14674886}.
FT   TRANSMEM     80    100       Helical. {ECO:0000255}.
FT   TOPO_DOM    101    139       Cytoplasmic.
FT                                {ECO:0000269|PubMed:14674886}.
FT   TRANSMEM    140    160       Helical. {ECO:0000255}.
FT   TOPO_DOM    161    170       Periplasmic.
FT                                {ECO:0000269|PubMed:14674886}.
FT   TRANSMEM    171    191       Helical. {ECO:0000255}.
FT   TOPO_DOM    192    287       Cytoplasmic.
FT                                {ECO:0000269|PubMed:14674886}.
FT   DOMAIN      217    247       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      251    280       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       226    226       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       229    229       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       232    232       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       236    236       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       260    260       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       263    263       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       266    266       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       270    270       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
SQ   SEQUENCE   287 AA;  31874 MW;  50AF7D5E0FFBC4D4 CRC64;
     MANRKRDAGR EALEKKGWWR SHRWLVLRRL CQFFVLGMFL SGPWFGVWIL HGNYSSSLLF
     DTVPLTDPLM TLQSLASGHL PATVALTGAV IITVLYALAG KRLFCSWVCP LNPITDLANW
     LRRRFDLNQS ATIPRHIRYV LLVVILVGSA LTGTLIWEWI NPVSLMGRSL VMGFGSGALL
     ILALFLFDLL VVEHGWCGHI CPVGALYGVL GSKGVITVAA TDRQKCNRCM DCFHVCPEPH
     VLRAPVLDEQ SPVQVTSRDC MTCGRCVDVC SEDVFTITTR WSSGAKS
//
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