位置:首页 > 蛋白库 > DMSD_SALTY
DMSD_SALTY
ID   DMSD_SALTY              Reviewed;         204 AA.
AC   Q8ZPK0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=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=STM1495;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS), AND SUBUNIT.
RX   PubMed=18175314; DOI=10.1002/prot.21828;
RA   Qiu Y., Zhang R., Binkowski T.A., Tereshko V., Joachimiak A.,
RA   Kossiakoff A.;
RT   "The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium,
RT   a proofreading chaperone on the Tat pathway.";
RL   Proteins 71:525-533(2008).
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   -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:18175314}.
CC   -!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00940}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006468; AAL20414.1; -; Genomic_DNA.
DR   RefSeq; NP_460455.1; NC_003197.2.
DR   RefSeq; WP_000206561.1; NC_003197.2.
DR   PDB; 1S9U; X-ray; 1.38 A; A=1-204.
DR   PDBsum; 1S9U; -.
DR   AlphaFoldDB; Q8ZPK0; -.
DR   SMR; Q8ZPK0; -.
DR   STRING; 99287.STM1495; -.
DR   PaxDb; Q8ZPK0; -.
DR   EnsemblBacteria; AAL20414; AAL20414; STM1495.
DR   GeneID; 1253013; -.
DR   KEGG; stm:STM1495; -.
DR   PATRIC; fig|99287.12.peg.1580; -.
DR   HOGENOM; CLU_077650_7_1_6; -.
DR   OMA; AWHLLPW; -.
DR   PhylomeDB; Q8ZPK0; -.
DR   BioCyc; SENT99287:STM1495-MON; -.
DR   EvolutionaryTrace; Q8ZPK0; -.
DR   Proteomes; UP000001014; 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   1: Evidence at protein level;
KW   3D-structure; Chaperone; Reference proteome.
FT   CHAIN           1..204
FT                   /note="Tat proofreading chaperone DmsD"
FT                   /id="PRO_0000211654"
FT   HELIX           1..5
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   TURN            6..8
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           9..22
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           31..39
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           50..60
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           68..76
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           88..92
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           101..112
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           128..140
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           144..154
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           156..169
FT                   /evidence="ECO:0007829|PDB:1S9U"
FT   HELIX           173..192
FT                   /evidence="ECO:0007829|PDB:1S9U"
SQ   SEQUENCE   204 AA;  23481 MW;  EFB2930376875EF1 CRC64;
     MTTFLQRDDF AVTARVLGAL FYYSPESHET APLVQALLND DWQAQWPLDA EALAPVAAMF
     KTHSEESLPQ AWQRLFIGPY ALPSPPWGSV WLDRESVLFG DSTLALRQWM RENGIQFEMQ
     QNEPEDHFGS LLLLAAWLAE NDRHHECEQL LAWHLFPWSS RFLDVFIDHA GHPFYQALGQ
     LARLTLAQWQ AQLIIPVAVK PLFR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024