NAPD_ECOLI
ID NAPD_ECOLI Reviewed; 87 AA.
AC P0A9I5; P33938;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Chaperone NapD {ECO:0000255|HAMAP-Rule:MF_02200, ECO:0000305};
DE AltName: Full=NapA signal peptide-binding chaperone NapD {ECO:0000255|HAMAP-Rule:MF_02200, ECO:0000305};
GN Name=napD {ECO:0000255|HAMAP-Rule:MF_02200}; Synonyms=yojF;
GN OrderedLocusNames=b2207, JW2195;
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 / 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 [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 DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=10548535; DOI=10.1042/bj3440069;
RA Potter L.C., Cole J.A.;
RT "Essential roles for the products of the napABCD genes, but not napFGH, in
RT periplasmic nitrate reduction by Escherichia coli K-12.";
RL Biochem. J. 344:69-76(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH NAPA.
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 [7]
RP FUNCTION, AND INTERACTION WITH NAPA.
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 [8] {ECO:0007744|PDB:2JSX}
RP STRUCTURE BY NMR, FUNCTION, SUBUNIT, INTERACTION WITH NAPA, AND SUBCELLULAR
RP LOCATION.
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 [9] {ECO:0007744|PDB:2PQ4}
RP STRUCTURE BY NMR IN COMPLEX WITH NAPA SIGNAL PEPTIDE.
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: Chaperone for NapA, the catalytic subunit of the periplasmic
CC nitrate reductase. It binds directly and specifically to the twin-
CC arginine signal peptide of NapA, preventing premature interaction with
CC the Tat translocase and premature export (PubMed:17901208,
CC PubMed:22329966). May have a role in the insertion of the NapA
CC molybdenum cofactor (PubMed:24314029). {ECO:0000269|PubMed:17901208,
CC ECO:0000269|PubMed:22329966, ECO:0000269|PubMed:24314029}.
CC -!- SUBUNIT: Monomer in solution (PubMed:17901208). Interacts with the
CC cytoplasmic NapA precursor (Ref.9, PubMed:17901208, PubMed:22329966,
CC PubMed:24314029). {ECO:0000269|PubMed:17901208,
CC ECO:0000269|PubMed:22329966, ECO:0000269|PubMed:24314029,
CC ECO:0000269|Ref.9}.
CC -!- INTERACTION:
CC P0A9I5; P33937: napA; NbExp=11; IntAct=EBI-554985, EBI-554952;
CC P0A9I5; P0A9M8: pta; NbExp=3; IntAct=EBI-554985, EBI-555015;
CC P0A9I5; P0A8E7: yajQ; NbExp=4; IntAct=EBI-554985, EBI-370752;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02200,
CC ECO:0000269|PubMed:17901208}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant lacks periplasmic nitrate
CC reductase activity, with either glycerol or formate as the electron
CC donor. {ECO:0000269|PubMed:10548535}.
CC -!- SIMILARITY: Belongs to the NapD family. {ECO:0000255|HAMAP-
CC Rule:MF_02200, 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; AAA16400.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75267.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15990.1; -; Genomic_DNA.
DR PIR; E64990; E64990.
DR RefSeq; NP_416711.1; NC_000913.3.
DR RefSeq; WP_000557378.1; NZ_STEB01000002.1.
DR PDB; 2JSX; NMR; -; A=1-87.
DR PDB; 2PQ4; NMR; -; A=1-87.
DR PDBsum; 2JSX; -.
DR PDBsum; 2PQ4; -.
DR AlphaFoldDB; P0A9I5; -.
DR BMRB; P0A9I5; -.
DR SMR; P0A9I5; -.
DR BioGRID; 4262220; 160.
DR BioGRID; 849573; 2.
DR DIP; DIP-46322N; -.
DR IntAct; P0A9I5; 22.
DR MINT; P0A9I5; -.
DR STRING; 511145.b2207; -.
DR TCDB; 3.D.11.1.1; the periplasmic nitrate reductase complex (nap) complex family.
DR PaxDb; P0A9I5; -.
DR PRIDE; P0A9I5; -.
DR EnsemblBacteria; AAC75267; AAC75267; b2207.
DR EnsemblBacteria; BAA15990; BAA15990; BAA15990.
DR GeneID; 67416643; -.
DR GeneID; 945187; -.
DR KEGG; ecj:JW2195; -.
DR KEGG; eco:b2207; -.
DR PATRIC; fig|1411691.4.peg.29; -.
DR EchoBASE; EB2064; -.
DR eggNOG; COG3062; Bacteria.
DR HOGENOM; CLU_155794_1_0_6; -.
DR InParanoid; P0A9I5; -.
DR OMA; ENQGFIT; -.
DR PhylomeDB; P0A9I5; -.
DR BioCyc; EcoCyc:NAPD-MON; -.
DR BioCyc; MetaCyc:NAPD-MON; -.
DR EvolutionaryTrace; P0A9I5; -.
DR PRO; PR:P0A9I5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0051224; P:negative regulation of protein transport; IDA:EcoCyc.
DR HAMAP; MF_02200; NapD; 1.
DR InterPro; IPR005623; Chaperone_NapD_NO3_reduct.
DR PANTHER; PTHR38603; PTHR38603; 1.
DR Pfam; PF03927; NapD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..87
FT /note="Chaperone NapD"
FT /id="PRO_0000096713"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:2JSX"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:2JSX"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2PQ4"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2JSX"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:2JSX"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:2JSX"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:2JSX"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:2JSX"
SQ SEQUENCE 87 AA; 9469 MW; EE59DF4EF17F650D CRC64;
MHTNWQVCSL VVQAKSERIS DISTQLNAFP GCEVAVSDAP SGQLIVVVEA EDSETLIQTI
ESVRNVEGVL AVSLVYHQQE EQGEETP
