ID B5XR81_KLEP3 Unreviewed; 202 AA.
AC B5XR81;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Tat proofreading chaperone DmsD {ECO:0000256|HAMAP-Rule:MF_00940};
DE AltName: Full=DMSO reductase maturation protein {ECO:0000256|HAMAP-Rule:MF_00940};
DE AltName: Full=Twin-arginine leader-binding protein DmsD {ECO:0000256|HAMAP-Rule:MF_00940};
GN Name=dmsD {ECO:0000256|HAMAP-Rule:MF_00940,
GN ECO:0000313|EMBL:ACI11201.1};
GN OrderedLocusNames=KPK_2878 {ECO:0000313|EMBL:ACI11201.1};
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI11201.1, ECO:0000313|Proteomes:UP000001734};
RN [1] {ECO:0000313|EMBL:ACI11201.1, ECO:0000313|Proteomes:UP000001734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:ACI11201.1,
RC ECO:0000313|Proteomes:UP000001734};
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(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:0000256|HAMAP-
CC Rule:MF_00940}.
CC -!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00940}.
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DR EMBL; CP000964; ACI11201.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XR81; -.
DR KEGG; kpe:KPK_2878; -.
DR HOGENOM; CLU_077650_7_1_6; -.
DR Proteomes; UP000001734; Chromosome.
DR GO; GO:0005048; F:signal sequence binding; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3480.10; TorD-like; 1.
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 PANTHER; PTHR34227; CHAPERONE PROTEIN YCDY; 1.
DR PANTHER; PTHR34227:SF6; TAT PROOFREADING CHAPERONE DMSD; 1.
DR Pfam; PF02613; Nitrate_red_del; 1.
DR PIRSF; PIRSF004690; DmsD; 1.
DR SUPFAM; SSF89155; TorD-like; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00940}.
SQ SEQUENCE 202 AA; 22405 MW; 2FCD79747ECA4F97 CRC64;
MMPIPNRDAV ALSARTLGAL FSYAPNSAHI APLVAAFQDG SWQQQWPFPV AAPQASAFAA
STEESLPEAW QRLFIGPWAL PAPPWGSVWL DKESVLFGDS TLALREWMRT NGIALDAERN
EPEDHFGTLL LLAAWLCETE QDALFAQLLA WHLLPWSGRF LSVFVDHAAH PFYQALGQLA
QATLAQWQEN LPIAVAEKAL YR
//
