ID   NAPD_SHIFL              Reviewed;          87 AA.
AC   P0A9I7; P33938;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Chaperone NapD {ECO:0000255|HAMAP-Rule:MF_02200};
DE   AltName: Full=NapA signal peptide-binding chaperone NapD {ECO:0000255|HAMAP-Rule:MF_02200};
GN   Name=napD {ECO:0000255|HAMAP-Rule:MF_02200};
GN   OrderedLocusNames=SF2291, S2421;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_02200}.
CC   -!- SUBUNIT: Interacts with the cytoplasmic NapA precursor.
CC       {ECO:0000255|HAMAP-Rule:MF_02200}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02200,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NapD family. {ECO:0000255|HAMAP-
CC       Rule:MF_02200}.
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DR   EMBL; AE005674; AAN43810.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17627.1; -; Genomic_DNA.
DR   RefSeq; NP_708103.1; NC_004337.2.
DR   RefSeq; WP_000557378.1; NZ_WPGW01000022.1.
DR   AlphaFoldDB; P0A9I7; -.
DR   BMRB; P0A9I7; -.
DR   SMR; P0A9I7; -.
DR   STRING; 198214.SF2291; -.
DR   EnsemblBacteria; AAN43810; AAN43810; SF2291.
DR   EnsemblBacteria; AAP17627; AAP17627; S2421.
DR   GeneID; 1027277; -.
DR   GeneID; 67416643; -.
DR   KEGG; sfl:SF2291; -.
DR   KEGG; sfx:S2421; -.
DR   PATRIC; fig|198214.7.peg.2742; -.
DR   HOGENOM; CLU_155794_1_0_6; -.
DR   OMA; ENQGFIT; -.
DR   OrthoDB; 1976760at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005048; F:signal sequence binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051224; P:negative regulation of protein transport; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02200; NapD; 1.
DR   InterPro; IPR005623; Chaperone_NapD_NO3_reduct.
DR   PANTHER; PTHR38603; PTHR38603; 1.
DR   Pfam; PF03927; NapD; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..87
FT                   /note="Chaperone NapD"
FT                   /id="PRO_0000096716"
SQ   SEQUENCE   87 AA;  9469 MW;  EE59DF4EF17F650D CRC64;
     MHTNWQVCSL VVQAKSERIS DISTQLNAFP GCEVAVSDAP SGQLIVVVEA EDSETLIQTI
     ESVRNVEGVL AVSLVYHQQE EQGEETP