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 27-MAR-2024, entry version 200. 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}; GN Synonyms=yojC, yojD, yojE; OrderedLocusNames=b2206, JW2194; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; 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; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 511145-b2206; -. DR EnsemblBacteria; AAC75266; AAC75266; b2206. 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; GMNAHQH; -. DR OrthoDB; 9816402at2; -. DR PhylomeDB; P33937; -. DR BioCyc; EcoCyc:NAPA-MONOMER; -. DR BioCyc; MetaCyc:NAPA-MONOMER; -. DR BRENDA; 1.9.6.1; 2026. DR EvolutionaryTrace; P33937; -. DR PHI-base; PHI:10522; -. 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; NAS:ComplexPortal. DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1. DR CDD; cd02754; MopB_Nitrate-R-NapA-like; 1. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 3.30.200.210; -; 1. DR Gene3D; 3.40.50.740; -; 1. DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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 NCBIfam; TIGR01706; NAPA; 1. DR NCBIfam; TIGR01409; TAT_signal_seq; 1. DR PANTHER; PTHR43105:SF11; PERIPLASMIC NITRATE REDUCTASE; 1. DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1. 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; ADC-like; 1. DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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 //