NAPD_PARPN
ID NAPD_PARPN Reviewed; 112 AA.
AC Q56349;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 59.
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};
OS Paracoccus pantotrophus (Thiosphaera pantotropha).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=82367;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 / NCCB
RC 82005 / GB17;
RX PubMed=7639719; DOI=10.1042/bj3090983;
RA Berks B.C., Richardson D.J., Reilly A., Willis A.C., Ferguson S.J.;
RT "The napEDABC gene cluster encoding the periplasmic nitrate reductase
RT system of Thiosphaera pantotropha.";
RL Biochem. J. 309:983-992(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; Z36773; CAA85345.1; -; Genomic_DNA.
DR PIR; S56138; S56138.
DR AlphaFoldDB; Q56349; -.
DR SMR; Q56349; -.
DR STRING; 935565.JAEM01000057_gene22; -.
DR eggNOG; COG3062; Bacteria.
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 Pfam; PF03927; NapD; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm.
FT CHAIN 1..112
FT /note="Chaperone NapD"
FT /id="PRO_0000096715"
SQ SEQUENCE 112 AA; 12123 MW; 9F725E498E8FE1F0 CRC64;
MREPDRTPIQ RRDILTGKLK QDSGGESRFL HISSAIVTAR PDRAADLARH FATLPGTEVH
AVQGAKIVLV LEGASVGEIR QPHGAISVME GVFSANLVFE QILPADEREA LS