NAPH_HAEIN
ID NAPH_HAEIN Reviewed; 287 AA.
AC P44653;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ferredoxin-type protein NapH {ECO:0000250|UniProtKB:P33934};
GN Name=napH; OrderedLocusNames=HI_0346;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Required for electron transfer from ubiquinol, via NapC, to
CC the periplasmic nitrate reductase NapAB complex.
CC {ECO:0000250|UniProtKB:P33934}.
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:0000250|UniProtKB:P33934}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P33934}; Multi-pass membrane protein
CC {ECO:0000255}.
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DR EMBL; L42023; AAC22007.1; -; Genomic_DNA.
DR PIR; B64149; B64149.
DR RefSeq; NP_438510.1; NC_000907.1.
DR RefSeq; WP_005694327.1; NC_000907.1.
DR AlphaFoldDB; P44653; -.
DR STRING; 71421.HI_0346; -.
DR EnsemblBacteria; AAC22007; AAC22007; HI_0346.
DR KEGG; hin:HI_0346; -.
DR PATRIC; fig|71421.8.peg.365; -.
DR eggNOG; COG0348; Bacteria.
DR HOGENOM; CLU_066585_1_0_6; -.
DR OMA; CPVGAFY; -.
DR PhylomeDB; P44653; -.
DR BioCyc; HINF71421:G1GJ1-362-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; PF12801; Fer4_5; 2.
DR Pfam; PF12837; Fer4_6; 1.
DR TIGRFAMs; TIGR02163; napH; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
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_0000159284"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P33934"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..79
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P33934"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P33934"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..170
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P33934"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P33934"
FT DOMAIN 217..247
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 252..281
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 261
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 264
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 267
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 271
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; 31753 MW; D2E20FC4E3C3C197 CRC64;
MANAPKFAGK ESREKWGWWY ANRFLFWRRL SQLSILAMFL SGPYFGVWIL KGNYSGSLLL
DTIPLSDPLI TAESLAARHL PDALTLIGAA IIVLFYAVLG SKVFCGWVCP LNVVTDCAAW
LRRKLGIRQT AKISRGLRYG ILVLILLGSS VSGMLLWEWV NPVAALGRAF VFGFGATGWL
LLVIFLFDLL IAEHGWCGHL CPIGAAYGVI GAKSLIRIKV IDRAKCDNCM DCYNVCPEAQ
VLRSPLHGKK DESLLVLSKD CISCGRCIDV CAEKVFKFST RFDHSGE
