TRAD2_ECOLX
ID TRAD2_ECOLX Reviewed; 738 AA.
AC P22708;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Coupling protein TraD;
DE AltName: Full=DNA transport protein TraD;
GN Name=traD;
OS Escherichia coli.
OG Plasmid IncFII R100 (NR1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2164585; DOI=10.1016/0022-2836(90)90145-c;
RA Yoshioka Y., Fujita Y., Ohtsubo E.;
RT "Nucleotide sequence of the promoter-distal region of the tra operon of
RT plasmid R100, including traI (DNA helicase I) and traD genes.";
RL J. Mol. Biol. 214:39-53(1990).
CC -!- FUNCTION: Conjugative DNA transfer (CDT) is the unidirectional transfer
CC of ssDNA plasmid from a donor to a recipient cell. It is the central
CC mechanism by which antibiotic resistance and virulence factors are
CC propagated in bacterial populations. Couples the transferosome to a
CC type IV secretion system. Probably forms a pore through which single-
CC stranded plasmid DNA is transferred to the secretion system. Plasmid
CC specificity is conferred by the TraD-TraM pair (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with relaxosome component TraM. May form a hexamer
CC in the membrane (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TrwB coupling protein family. {ECO:0000305}.
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DR EMBL; X55815; CAA39336.1; -; Genomic_DNA.
DR PIR; S10659; S10659.
DR RefSeq; WP_000009331.1; NZ_UEFE01000037.1.
DR AlphaFoldDB; P22708; -.
DR SMR; P22708; -.
DR PATRIC; fig|562.9739.peg.5216; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd01127; TrwB; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014128; T4SS_TraD.
DR InterPro; IPR019476; T4SS_TraD_DNA-bd.
DR InterPro; IPR022585; TraD_N.
DR Pfam; PF12615; TraD_N; 1.
DR Pfam; PF10412; TrwB_AAD_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02759; TraD_Ftype; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Conjugation; Membrane;
KW Nucleotide-binding; Plasmid; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..738
FT /note="Coupling protein TraD"
FT /id="PRO_0000068449"
FT TRANSMEM 28..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 617..619
FT /note="1"
FT REPEAT 620..622
FT /note="2"
FT REPEAT 623..625
FT /note="3"
FT REPEAT 626..628
FT /note="4"
FT REPEAT 629..631
FT /note="5"
FT REPEAT 632..634
FT /note="6"
FT REPEAT 635..637
FT /note="7"
FT REPEAT 638..640
FT /note="8"
FT REPEAT 641..643
FT /note="9"
FT REPEAT 644..646
FT /note="10"
FT REGION 607..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..646
FT /note="10 X 3 AA tandem repeats of [QE]-Q-P"
FT COMPBIAS 624..641
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 738 AA; 83901 MW; 84CB1F48245E766F CRC64;
MSFNAKDMTQ GGQIASMRIR MFSQIANIML YCLFIFFWIL IGLVLWVKIS WQTFINGCIY
WWCTSLEGMR DLIKSQPVYE IQYYGKTFRM NAAQVLHDKY MIWCGEQLWS AFVLASVVAL
VICLITFFVV SWILGRQGKQ QSENEVTGGR QLTDNPKDVA RMLKKDGKDS DIRIGDLPII
RDSEIQNFCL HGTVGAGKSE VIRRLANYAR QRGDMVVIYD RSGEFVKSYY DPSIDKILNP
LDARCAAWDL WKECLTQPDF DNTANTLIPM GTKEDPFWQG SGRTIFAEAA YLMRNDPNRS
YSKLVDTLLS IKIEKLRTFL RNSPAANLVE EKIEKTAISI RAVLTNYVKA IRYLQGIEHN
GDPFTIRDWM RGVREDQKNG WLFISSNADT HASLKPVISM WLSIAIRGLL AMGENRNRRV
WFFCDELPTL HKLPDLVEIL PEARKFGGCY VFGIQSYAQL EDIYGEKAAA TLFDVMNTRA
FFRSPSHKIA EFAAGEIGEK EHLKASEQYS YGADPVRDGV STGKDMERQT LVSYSDIQSL
PDLTCYVTLP GPYPAVKLSL KYQARPKVAP EFIPRDINPE MENRLSAVLA AREAEGRQMA
SLFEPEVASG EDVTQAEQPQ QPQQPQQPQQ PQQPQQPQQP QQPQQPVSSV INDKKSDAGV
SVPAGGIEQE LKMKPEEEME QQLPPGISES GEVVDMAAYE AWQQENHPDI QQHMQRREEV
NINVHRERGE DVEPGDDF