NAPH_ECOLI
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 03-AUG-2022, entry version 161.
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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11967083; DOI=10.1046/j.1365-2958.2002.02875.x;
RA Brondijk T.H., Fiegen D., Richardson D.J., Cole J.A.;
RT "Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic
RT 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 coli
RT K-12: location, topology and physiological roles in quinol oxidation and
RT 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, to
CC 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-ProRule:PRU00711};
CC -!- SUBUNIT: Interacts with NapC. {ECO:0000269|PubMed:14674886}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:14674886,
CC ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14674886}.
CC -!- DISRUPTION PHENOTYPE: Deletion of both napG and napH genes has little
CC effect on the overall rate of nitrate reduction during growth in the
CC glycerol/nitrate medium. However, during growth in the glucose/nitrate
CC medium, the double mutant shows a decreased rate of electron transfer
CC that correlates with decreased NapAB activity.
CC {ECO:0000269|PubMed:11967083}.
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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_STEB01000002.1.
DR AlphaFoldDB; 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 jPOST; P33934; -.
DR PaxDb; P33934; -.
DR PRIDE; P33934; -.
DR EnsemblBacteria; AAC75264; AAC75264; b2204.
DR EnsemblBacteria; BAE76667; BAE76667; BAE76667.
DR GeneID; 66673901; -.
DR GeneID; 945984; -.
DR KEGG; ecj:JW2192; -.
DR KEGG; eco:b2204; -.
DR PATRIC; fig|1411691.4.peg.32; -.
DR EchoBASE; EB1992; -.
DR eggNOG; COG0348; Bacteria.
DR HOGENOM; CLU_066585_1_0_6; -.
DR InParanoid; P33934; -.
DR OMA; CPVGAFY; -.
DR PhylomeDB; P33934; -.
DR BioCyc; EcoCyc:NAPH-MON; -.
DR BioCyc; MetaCyc:NAPH-MON; -.
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 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; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..287
FT /note="Ferredoxin-type protein NapH"
FT /id="PRO_0000159283"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:14674886"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..79
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:14674886"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:14674886"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..170
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:14674886"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:14674886"
FT DOMAIN 217..247
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 251..280
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 226
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 229
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 236
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 266
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 270
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="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
