ID   NAPD_HAEIN              Reviewed;          93 AA.
AC   P44651;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 104.
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}; OrderedLocusNames=HI_0343;
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: 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; L42023; AAC22005.1; -; Genomic_DNA.
DR   PIR; I64148; I64148.
DR   RefSeq; NP_438507.1; NC_000907.1.
DR   RefSeq; WP_005694331.1; NC_000907.1.
DR   AlphaFoldDB; P44651; -.
DR   SMR; P44651; -.
DR   STRING; 71421.HI_0343; -.
DR   EnsemblBacteria; AAC22005; AAC22005; HI_0343.
DR   KEGG; hin:HI_0343; -.
DR   PATRIC; fig|71421.8.peg.361; -.
DR   eggNOG; COG3062; Bacteria.
DR   HOGENOM; CLU_155794_1_0_6; -.
DR   OMA; ENQGFIT; -.
DR   PhylomeDB; P44651; -.
DR   BioCyc; HINF71421:G1GJ1-359-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR   GO; GO:0051224; P:negative regulation of protein transport; IBA:GO_Central.
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..93
FT                   /note="Chaperone NapD"
FT                   /id="PRO_0000096714"
SQ   SEQUENCE   93 AA;  10516 MW;  6CF771F31660446F CRC64;
     MNNTNLILEN ARDWHVVGLI VQGNPKKLSA IQTALLAIEH TEIPTLDEKL GKFVVVMQSN
     DQHLLLEKME SVKDIDGVIN VSLVYHEQDE QNK