NAPA_ECOLI
ID NAPA_ECOLI Reviewed; 828 AA.
AC P33937; P78087;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630, ECO:0000305};
DE EC=1.9.6.1 {ECO:0000255|HAMAP-Rule:MF_01630, ECO:0000269|PubMed:17130127};
DE Flags: Precursor;
GN Name=napA {ECO:0000255|HAMAP-Rule:MF_01630}; Synonyms=yojC, yojD, yojE;
GN OrderedLocusNames=b2206, JW2194;
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 SEQUENCE REVISION.
RA Robison K.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-757.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [6]
RP PROTEIN SEQUENCE OF 37-43, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=10234835; DOI=10.1111/j.1574-6968.1999.tb13564.x;
RA Thomas G., Potter L., Cole J.A.;
RT "The periplasmic nitrate reductase from Escherichia coli: a heterodimeric
RT molybdoprotein with a double-arginine signal sequence and an unusual leader
RT peptide cleavage site.";
RL FEMS Microbiol. Lett. 174:167-171(1999).
RN [7]
RP INTERACTION WITH NAPD AND NAPF.
RC STRAIN=K12;
RX PubMed=17074894; DOI=10.1099/mic.0.29157-0;
RA Nilavongse A., Brondijk T.H., Overton T.W., Richardson D.J., Leach E.R.,
RA Cole J.A.;
RT "The NapF protein of the Escherichia coli periplasmic nitrate reductase
RT system: demonstration of a cytoplasmic location and interaction with the
RT catalytic subunit, NapA.";
RL Microbiology 152:3227-3237(2006).
RN [8]
RP EXPORT VIA THE TAT-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [9]
RP ACTIVITY REGULATION, AND INTERACTION WITH NAPD.
RX PubMed=17901208; DOI=10.1073/pnas.0703967104;
RA Maillard J., Spronk C.A., Buchanan G., Lyall V., Richardson D.J.,
RA Palmer T., Vuister G.W., Sargent F.;
RT "Structural diversity in twin-arginine signal peptide-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15641-15646(2007).
RN [10]
RP INTERACTION WITH NAPD, AND MUTAGENESIS OF ARG-6; LYS-10 AND ALA-17.
RX PubMed=22329966; DOI=10.1111/j.1365-2958.2012.08005.x;
RA Grahl S., Maillard J., Spronk C.A., Vuister G.W., Sargent F.;
RT "Overlapping transport and chaperone-binding functions within a bacterial
RT twin-arginine signal peptide.";
RL Mol. Microbiol. 83:1254-1267(2012).
RN [11]
RP INTERACTION WITH NAPD, AND DOMAIN.
RX PubMed=24314029; DOI=10.1111/febs.12592;
RA Dow J.M., Grahl S., Ward R., Evans R., Byron O., Norman D.G., Palmer T.,
RA Sargent F.;
RT "Characterization of a periplasmic nitrate reductase in complex with its
RT biosynthetic chaperone.";
RL FEBS J. 281:246-260(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 37-828 IN COMPLEX WITH
RP IRON-SULFUR (4FE-4S) AND MOLYBDENUM MOLYBDOPTERIN COFACTOR, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND INTERACTION WITH NAPB.
RX PubMed=17130127; DOI=10.1074/jbc.m607353200;
RA Jepson B.J., Mohan S., Clarke T.A., Gates A.J., Cole J.A., Butler C.S.,
RA Butt J.N., Hemmings A.M., Richardson D.J.;
RT "Spectropotentiometric and structural analysis of the periplasmic nitrate
RT reductase from Escherichia coli.";
RL J. Biol. Chem. 282:6425-6437(2007).
RN [13]
RP STRUCTURE BY NMR OF 1-35 IN COMPLEX WITH NAPD.
RA Minailiuc O.M., Ekiel I., Cheng J., Milad M., Gandhi S., Larocque R.,
RA Cygler M., Matte A.;
RT "Solution structure of NapD, a private chaperone of periplasmic nitrate
RT reductase NapA/B, in complex with NapA1-35 signal peptide.";
RL Submitted (MAY-2007) to the PDB data bank.
CC -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC complex NapAB. Receives electrons from NapB and catalyzes the reduction
CC of nitrate to nitrite. {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:17130127}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome] + 2 H(+) + nitrate = 2 Fe(III)-
CC [cytochrome] + H2O + nitrite; Xref=Rhea:RHEA:12909, Rhea:RHEA-
CC COMP:11777, Rhea:RHEA-COMP:11778, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.6.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:17130127};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:17130127};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:17130127};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:17130127};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:17130127};
CC -!- ACTIVITY REGULATION: Interaction in the cytoplasm with the NapD
CC chaperone prevents premature export. {ECO:0000269|PubMed:17901208}.
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB (PubMed:10234835, PubMed:17130127). Before
CC export to the periplasm, the NapA twin-arginine signal sequence
CC interacts with NapD and NapF (PubMed:17074894, PubMed:17901208,
CC PubMed:22329966, PubMed:24314029, Ref.13).
CC {ECO:0000269|PubMed:10234835, ECO:0000269|PubMed:17074894,
CC ECO:0000269|PubMed:17130127, ECO:0000269|PubMed:17901208,
CC ECO:0000269|PubMed:22329966, ECO:0000269|PubMed:24314029,
CC ECO:0000269|Ref.13}.
CC -!- INTERACTION:
CC P33937; P0ABL3: napB; NbExp=2; IntAct=EBI-554952, EBI-17171907;
CC P33937; P0A9I5: napD; NbExp=11; IntAct=EBI-554952, EBI-554985;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:10234835}.
CC -!- DOMAIN: The twin-arginine signal peptide of NapA is structured in its
CC unbound form and undergoes a small but significant conformational
CC change upon interaction with NapD. {ECO:0000269|PubMed:24314029}.
CC -!- PTM: Exported by the Tat system (PubMed:17218314). The position of the
CC signal peptide cleavage has been experimentally proven
CC (PubMed:10234835). {ECO:0000269|PubMed:10234835,
CC ECO:0000269|PubMed:17218314}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01630, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16399.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00008; AAA16399.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75266.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15989.2; -; Genomic_DNA.
DR PIR; D64990; D64990.
DR RefSeq; NP_416710.1; NC_000913.3.
DR RefSeq; WP_000778061.1; NZ_SSZK01000027.1.
DR PDB; 2NYA; X-ray; 2.50 A; A/F=37-828.
DR PDB; 2PQ4; NMR; -; B=1-35.
DR PDBsum; 2NYA; -.
DR PDBsum; 2PQ4; -.
DR AlphaFoldDB; P33937; -.
DR SMR; P33937; -.
DR BioGRID; 4262221; 162.
DR BioGRID; 851429; 1.
DR ComplexPortal; CPX-3447; NapAB nitrate reductase complex.
DR DIP; DIP-10304N; -.
DR IntAct; P33937; 14.
DR MINT; P33937; -.
DR STRING; 511145.b2206; -.
DR TCDB; 3.D.11.1.1; the periplasmic nitrate reductase complex (nap) complex family.
DR jPOST; P33937; -.
DR PaxDb; P33937; -.
DR PRIDE; P33937; -.
DR EnsemblBacteria; AAC75266; AAC75266; b2206.
DR EnsemblBacteria; BAA15989; BAA15989; BAA15989.
DR GeneID; 947093; -.
DR KEGG; ecj:JW2194; -.
DR KEGG; eco:b2206; -.
DR PATRIC; fig|1411691.4.peg.30; -.
DR EchoBASE; EB1994; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_6; -.
DR InParanoid; P33937; -.
DR OMA; KIVSFWT; -.
DR PhylomeDB; P33937; -.
DR BioCyc; EcoCyc:NAPA-MON; -.
DR BioCyc; MetaCyc:NAPA-MON; -.
DR BRENDA; 1.9.6.1; 2026.
DR EvolutionaryTrace; P33937; -.
DR PRO; PR:P33937; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009325; C:nitrate reductase complex; IPI:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:CACAO.
DR GO; GO:0042597; C:periplasmic space; IDA:ComplexPortal.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:EcoCyc.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0050140; F:nitrate reductase (cytochrome) activity; IEA:UniProtKB-EC.
DR GO; GO:0008940; F:nitrate reductase activity; IDA:CACAO.
DR GO; GO:0009061; P:anaerobic respiration; IGI:EcoliWiki.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042128; P:nitrate assimilation; IC:ComplexPortal.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR HAMAP; MF_01630; Nitrate_reduct_NapA; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01706; NAPA; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation;
KW Oxidoreductase; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..36
FT /note="Tat-type signal"
FT /evidence="ECO:0000269|PubMed:10234835"
FT CHAIN 37..828
FT /note="Periplasmic nitrate reductase"
FT /id="PRO_0000019170"
FT DOMAIN 39..95
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 83
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 150
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 175
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 179
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 212..219
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 243..247
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 262..264
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 372
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 376
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 482
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 508..509
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 531
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 558
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 718..727
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 794
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81186, ECO:0000255|HAMAP-
FT Rule:MF_01630"
FT BINDING 802
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT BINDING 819
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:17130127, ECO:0007744|PDB:2NYA"
FT MUTAGEN 6
FT /note="R->Q: Impairs interaction with NapD. Lack of nitrate
FT reductase activity. Tat transport is blocked."
FT /evidence="ECO:0000269|PubMed:22329966"
FT MUTAGEN 10
FT /note="K->Q: Impairs interaction with NapD. Slight decrease
FT in nitrate reductase activity. Minor defect in Tat
FT transport."
FT /evidence="ECO:0000269|PubMed:22329966"
FT MUTAGEN 17
FT /note="A->L: Impairs interaction with NapD."
FT /evidence="ECO:0000269|PubMed:22329966"
FT MUTAGEN 17
FT /note="A->Q: Impairs interaction with NapD. Decrease in
FT nitrate reductase activity. Defect in Tat transport."
FT /evidence="ECO:0000269|PubMed:22329966"
FT CONFLICT 98
FT /note="T -> R (in Ref. 1; AAA16399)"
FT /evidence="ECO:0000305"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:2PQ4"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2PQ4"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 338..345
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 349..360
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 380..394
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 411..416
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 436..446
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 461..469
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 483..486
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 490..493
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 494..499
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 504..511
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 514..517
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 519..525
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 558..565
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 591..595
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 599..602
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 616..621
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 625..637
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 638..641
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 647..650
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 672..674
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 694..698
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 710..712
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 714..719
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 735..738
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 750..754
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 755..757
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 763..768
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 771..782
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 789..793
FT /evidence="ECO:0007829|PDB:2NYA"
FT HELIX 801..803
FT /evidence="ECO:0007829|PDB:2NYA"
FT TURN 811..813
FT /evidence="ECO:0007829|PDB:2NYA"
FT STRAND 821..826
FT /evidence="ECO:0007829|PDB:2NYA"
SQ SEQUENCE 828 AA; 93042 MW; CE2D7AB000FEAFCA CRC64;
MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ
QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP LLRMKNGKYD KEGEFTPITW
DQAFDVMEEK FKTALKEKGP ESIGMFGSGQ WTIWEGYAAS KLFKAGFRSN NIDPNARHCM
ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGANMAEMH PILWSRITNR RLSNQNVTVA
VLSTYQHRSF ELADNGIIFT PQSDLVILNY IANYIIQNNA INQDFFSKHV NLRKGATDIG
YGLRPTHPLE KAAKNPGSDA SEPMSFEDYK AFVAEYTLEK TAEMTGVPKD QLEQLAQLYA
DPNKKVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV
GTFAHRLPAD MVVTNEKHRD ICEKKWNIPS GTIPAKIGLH AVAQDRALKD GKLNVYWTMC
TNNMQAGPNI NEERMPGWRD PRNFIIVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER
RTQFWRQQVQ APGEAKSDLW QLVQFSRRFK TEEVWPEDLL AKKPELRGKT LYEVLYATPE
VSKFPVSELA EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HKARGLRWPV
VNGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAEAPDE EYDLWLSTGR
VLEHWHTGSM TRRVPELHRA FPEAVLFIHP LDAKARDLRR GDKVKVVSRR GEVISIVETR
GRNRPPQGLV YMPFFDAAQL VNKLTLDATD PLSKETDFKK CAVKLEKV
