ID   PCRD_DECAR              Reviewed;         224 AA.
AC   Q47CW9;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Perchlorate reductase assembly chaperone protein;
GN   Name=pcrD; OrderedLocusNames=Daro_2581;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
RN   [2]
RP   IDENTIFICATION, GENE NAME, AND PREDICTED FUNCTION.
RX   PubMed=16030201; DOI=10.1128/jb.187.15.5090-5096.2005;
RA   Bender K.S., Shang C., Chakraborty R., Belchik S.M., Coates J.D.,
RA   Achenbach L.A.;
RT   "Identification, characterization, and classification of genes encoding
RT   perchlorate reductase.";
RL   J. Bacteriol. 187:5090-5096(2005).
CC   -!- FUNCTION: May function as a system-specific molybdenum chaperone
CC       protein essential for the assembly of the perchlorate reductase PcrAB
CC       complex prior to its periplasmic translocation via the Tat pathway.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type II DMSO reductase enzyme chaperone
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ47312.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000089; AAZ47312.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_049758697.1; NC_007298.1.
DR   AlphaFoldDB; Q47CW9; -.
DR   STRING; 159087.Daro_2581; -.
DR   EnsemblBacteria; AAZ47312; AAZ47312; Daro_2581.
DR   KEGG; dar:Daro_2581; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_1232968_0_0_4; -.
DR   OrthoDB; 1995553at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR   InterPro; IPR017843; DMSO_Rdtase_II_chaperone.
DR   InterPro; IPR036411; TorD-like_sf.
DR   Pfam; PF02613; Nitrate_red_del; 1.
DR   SUPFAM; SSF89155; SSF89155; 1.
DR   TIGRFAMs; TIGR03482; DMSO_red_II_cha; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm.
FT   CHAIN           1..224
FT                   /note="Perchlorate reductase assembly chaperone protein"
FT                   /id="PRO_0000422922"
SQ   SEQUENCE   224 AA;  25340 MW;  08D51B2DC6F927A4 CRC64;
     MNTLNDEAVV ERIDKSLARS RVYSLLAIGL GFPDVESHAG FSDGRLMIEM HQALEVCMPG
     LAEYFSEQIA PRLKLTCSFE DFEALFLTAF ETNMPVPSAA LYEGVHVQQS NRPGLILELK
     GFYRNFGLTM DAQGNELEDT LTAELEFMHF LTAKQAQAEM ESLSPNAYQR AQRDFLERHL
     VVWLPLVRAE VNAKVATQFF VALIDLAERF VDAHLEEMLF ELNS