ID   DMSD_HAEIN              Reviewed;         203 AA.
AC   P44102;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable Tat proofreading chaperone DmsD {ECO:0000255|HAMAP-Rule:MF_00940};
DE   AltName: Full=DMSO reductase maturation protein {ECO:0000255|HAMAP-Rule:MF_00940};
DE   AltName: Full=Twin-arginine leader-binding protein DmsD {ECO:0000255|HAMAP-Rule:MF_00940};
GN   Name=dmsD {ECO:0000255|HAMAP-Rule:MF_00940}; OrderedLocusNames=HI_1044;
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: Required for biogenesis/assembly of DMSO reductase, but not
CC       for the interaction of the DmsA signal peptide with the Tat system. May
CC       be part of a chaperone cascade complex that facilitates a folding-
CC       maturation pathway for the substrate protein. {ECO:0000255|HAMAP-
CC       Rule:MF_00940}.
CC   -!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00940}.
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DR   EMBL; L42023; AAC22703.1; -; Genomic_DNA.
DR   PIR; C64019; C64019.
DR   RefSeq; NP_439203.1; NC_000907.1.
DR   RefSeq; WP_005693380.1; NC_000907.1.
DR   AlphaFoldDB; P44102; -.
DR   SMR; P44102; -.
DR   STRING; 71421.HI_1044; -.
DR   EnsemblBacteria; AAC22703; AAC22703; HI_1044.
DR   KEGG; hin:HI_1044; -.
DR   PATRIC; fig|71421.8.peg.1089; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_077650_7_1_6; -.
DR   OMA; AWHLLPW; -.
DR   PhylomeDB; P44102; -.
DR   BioCyc; HINF71421:G1GJ1-1083-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005048; F:signal sequence binding; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00940; DmsD_chaperone; 1.
DR   InterPro; IPR026269; DmsD-type.
DR   InterPro; IPR028611; DmsD_chaperone.
DR   InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR   InterPro; IPR036411; TorD-like_sf.
DR   Pfam; PF02613; Nitrate_red_del; 1.
DR   PIRSF; PIRSF004690; DmsD; 1.
DR   SUPFAM; SSF89155; SSF89155; 1.
PE   3: Inferred from homology;
KW   Chaperone; Reference proteome.
FT   CHAIN           1..203
FT                   /note="Probable Tat proofreading chaperone DmsD"
FT                   /id="PRO_0000211656"
SQ   SEQUENCE   203 AA;  24082 MW;  D1DB97790FEAA681 CRC64;
     MQNTLQQISI YGRLLGAVFY YEPNDARLTD ILTFFRQPNW MQEWEISFDV KTHKKITALI
     EKGLQQNITE QYQYLFIGPN ELPTPPWGSV YLDPECVIFG NSLLALRDFL QQHQIAFQTQ
     QDEPEDHIGL MLMLAAYLAE NRPHLLTKFL REHFLTWAYH FLEQLSKIEN SDFYQALALL
     TIKTLQQWQV DLHINVPTVR FYR