TRAD1_ECOLI
ID TRAD1_ECOLI Reviewed; 717 AA.
AC P09130; O87742;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 4.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Coupling protein TraD;
DE AltName: Full=DNA transport protein TraD;
GN Name=traD; OrderedLocusNames=ECOK12F102;
OS Escherichia coli (strain K12).
OG Plasmid F, and Plasmid p1658/97.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12; PLASMID=F;
RX PubMed=2680768; DOI=10.1016/0378-1119(89)90179-0;
RA Jalajakumari M.B., Manning P.A.;
RT "Nucleotide sequence of the traD region in the Escherichia coli F sex
RT factor.";
RL Gene 81:195-202(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=F;
RX PubMed=7915817; DOI=10.1128/mr.58.2.162-210.1994;
RA Frost L.S., Ippen-Ihler K., Skurray R.A.;
RT "Analysis of the sequence and gene products of the transfer region of the F
RT sex factor.";
RL Microbiol. Rev. 58:162-210(1994).
RN [3]
RP SEQUENCE REVISION TO 190; 269-270 AND 321-325, AND VARIANT LEU-396.
RC PLASMID=F;
RX PubMed=10464182; DOI=10.1128/jb.181.17.5149-5159.1999;
RA Anthony K.G., Klimke W.A., Manchak J., Frost L.S.;
RT "Comparison of proteins involved in pilus synthesis and mating pair
RT stabilization from the related plasmids F and R100-1: insights into the
RT mechanism of conjugation.";
RL J. Bacteriol. 181:5149-5159(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=F;
RA Krause S., Lanka E.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / CR63; PLASMID=F;
RA Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
RT "Complete nucleotide sequence of the F plasmid: its implications for
RT organization and diversification of plasmid genomes.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=p1658/97;
RA Zienkiewicz M., Kern-Zdanowicz I., Golebiewski M., Ceglowski P.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RC STRAIN=K12; PLASMID=F;
RX PubMed=3323526; DOI=10.1016/0022-2836(87)90452-9;
RA Jalajakumari M.B., Guidolin A., Buhj H.J., Manning P.A.;
RT "Surface exclusion genes traS and traT of the F sex factor of Escherichia
RT coli K-12. Determination of the nucleotide sequence and promoter and
RT terminator activities.";
RL J. Mol. Biol. 198:1-11(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102 AND 665-717.
RC PLASMID=F;
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).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-717.
RC PLASMID=F;
RX PubMed=2163400; DOI=10.1128/jb.172.7.4127-4131.1990;
RA Bradshaw H.D. Jr., Traxler B.A., Minkley E.G. Jr., Nester E.W.,
RA Gordon M.P.;
RT "Nucleotide sequence of the traI (helicase I) gene from the sex factor F.";
RL J. Bacteriol. 172:4127-4131(1990).
RN [10]
RP CHARACTERIZATION.
RC PLASMID=F;
RX PubMed=1618779; DOI=10.1016/s0021-9258(18)42341-1;
RA Panicker M.M., Minkley E.G. Jr.;
RT "Purification and properties of the F sex factor TraD protein, an inner
RT membrane conjugal transfer protein.";
RL J. Biol. Chem. 267:12761-12766(1992).
RN [11]
RP INTERACTION WITH TRAM, AND SUBCELLULAR LOCATION.
RC PLASMID=F;
RX PubMed=9324263; DOI=10.1128/jb.179.19.6133-6137.1997;
RA Disque-Kochem C., Dreiseikelmann B.;
RT "The cytoplasmic DNA-binding protein TraM binds to the inner membrane
RT protein TraD in vitro.";
RL J. Bacteriol. 179:6133-6137(1997).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF 681-TRP--PHE-717.
RC PLASMID=F;
RX PubMed=9811665; DOI=10.1128/jb.180.22.6039-6042.1998;
RA Sastre J.I., Cabezon E., de la Cruz F.;
RT "The carboxyl terminus of protein TraD adds specificity and efficiency to
RT F-plasmid conjugative transfer.";
RL J. Bacteriol. 180:6039-6042(1998).
RN [13]
RP TOPOLOGY.
RC PLASMID=F;
RX PubMed=10498725; DOI=10.1128/jb.181.19.6108-6113.1999;
RA Lee M.H., Kosuk N., Bailey J., Traxler B., Manoil C.;
RT "Analysis of F factor TraD membrane topology by use of gene fusions and
RT trypsin-sensitive insertions.";
RL J. Bacteriol. 181:6108-6113(1999).
RN [14]
RP INTERACTION WITH TRAM.
RC PLASMID=F;
RX PubMed=15995191; DOI=10.1128/jb.187.14.4767-4773.2005;
RA Lu J., Frost L.S.;
RT "Mutations in the C-terminal region of TraM provide evidence for in vivo
RT TraM-TraD interactions during F-plasmid conjugation.";
RL J. Bacteriol. 187:4767-4773(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 708-717 IN COMPLEX WITH
RP C-TERMINUS OF TRAM, AND MUTAGENESIS OF 710-ASP--PHE-717; GLU-712; ASP-715
RP AND PHE-717.
RC PLASMID=F;
RX PubMed=18717787; DOI=10.1111/j.1365-2958.2008.06391.x;
RA Lu J., Wong J.J., Edwards R.A., Manchak J., Frost L.S., Glover J.N.;
RT "Structural basis of specific TraD-TraM recognition during F plasmid-
RT mediated bacterial conjugation.";
RL Mol. Microbiol. 70:89-99(2008).
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. The last
CC 37 residues are important for determining plasmid specificity and
CC transfer efficiency, with additional specificity conferred by the TraD-
CC TraM pair. {ECO:0000269|PubMed:9811665}.
CC -!- SUBUNIT: Interacts with relaxosome component TraM. May form a hexamer
CC in the membrane. {ECO:0000269|PubMed:15995191,
CC ECO:0000269|PubMed:18717787, ECO:0000269|PubMed:9324263}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9324263};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9324263}.
CC -!- SIMILARITY: Belongs to the TrwB coupling protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC44181.2; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA30013.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M29254; AAA83928.1; -; Genomic_DNA.
DR EMBL; U01159; AAC44181.2; ALT_TERM; Genomic_DNA.
DR EMBL; AJ011707; CAA09749.1; -; Genomic_DNA.
DR EMBL; AP001918; BAA97972.1; -; Genomic_DNA.
DR EMBL; AF550679; AAO49544.1; -; Genomic_DNA.
DR EMBL; X06915; CAA30013.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X57428; CAA40674.1; -; Genomic_DNA.
DR EMBL; X57431; CAA40678.1; -; Genomic_DNA.
DR EMBL; M54796; AAA98083.1; -; Genomic_DNA.
DR PIR; JS0293; BVECAD.
DR RefSeq; NP_061481.1; NC_002483.1.
DR RefSeq; NP_862947.1; NC_004998.1.
DR RefSeq; WP_000009350.1; NZ_CP014273.1.
DR RefSeq; YP_009060132.1; NC_024956.1.
DR RefSeq; YP_009062862.1; NC_025014.1.
DR RefSeq; YP_009068320.1; NC_025139.1.
DR RefSeq; YP_009070586.1; NC_025175.1.
DR PDB; 3D8A; X-ray; 2.55 A; S/T/U/V/W/X/Y/Z=708-717.
DR PDBsum; 3D8A; -.
DR AlphaFoldDB; P09130; -.
DR SMR; P09130; -.
DR DIP; DIP-27652N; -.
DR PRIDE; P09130; -.
DR PATRIC; fig|83333.107.peg.610; -.
DR EvolutionaryTrace; P09130; -.
DR PRO; PR:P09130; -.
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 GO; GO:0009291; P:unidirectional conjugation; IMP:CACAO.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Conjugation;
KW Membrane; Nucleotide-binding; Plasmid; Transmembrane; Transmembrane helix.
FT CHAIN 1..717
FT /note="Coupling protein TraD"
FT /id="PRO_0000068448"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10498725"
FT TRANSMEM 28..47
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 48..104
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10498725"
FT TRANSMEM 105..130
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 131..717
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10498725"
FT REGION 614..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..634
FT /note="Polar 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"
FT VARIANT 396
FT /note="P -> L (in traD39; temperature-sensitive)"
FT /evidence="ECO:0000269|PubMed:10464182"
FT MUTAGEN 681..717
FT /note="WQQENHPDIQQQMQRREEVNINVHRERGEDVEPGDDF->CNRKIIRTSSSRC
FT SVVKR: 1000-fold increase in the transfer frequency of
FT plasmids R388 and RSF1010, a 10,000-fold reduction in F
FT plasmid transfer frequency."
FT /evidence="ECO:0000269|PubMed:9811665"
FT MUTAGEN 710..717
FT /note="Missing: Loss of interaction with TraM, 1000-fold
FT decrease in conjugation."
FT /evidence="ECO:0000269|PubMed:18717787"
FT MUTAGEN 712
FT /note="E->K: No change in conjugation efficiency. Partially
FT rescues a TraM K-99 mutation."
FT /evidence="ECO:0000269|PubMed:18717787"
FT MUTAGEN 715
FT /note="D->K: 10-fold decrease in conjugation efficiency."
FT /evidence="ECO:0000269|PubMed:18717787"
FT MUTAGEN 717
FT /note="F->A: 5000-fold decrease in conjugation efficiency."
FT /evidence="ECO:0000269|PubMed:18717787"
FT MUTAGEN 717
FT /note="F->FG: 1000-fold decrease in conjugation
FT efficiency."
FT /evidence="ECO:0000269|PubMed:18717787"
FT CONFLICT 19..62
FT /note="IRMFSQIANIMLYCLFIFFWILVGLVLWIKISWQTFVNGCIYWW -> YPHV
FT QPDRQYHALLPVYFFLDTRWSGFMDKISWTDVVNGLFTV (in Ref. 1;
FT AAA83928)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="L -> R (in Ref. 1; AAA83928)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..270
FT /note="PM -> RD (in Ref. 1; AAA83928)"
FT /evidence="ECO:0000305"
FT CONFLICT 321..325
FT /note="RNSPA -> VIHRQ (in Ref. 1; AAA83928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 81489 MW; EA43168766F3E6F3 CRC64;
MSFNAKDMTQ GGQIASMRIR MFSQIANIML YCLFIFFWIL VGLVLWIKIS WQTFVNGCIY
WWCTTLEGMR DLIKSQPVYE IQYYGKTFRM NAAQVLHDKY MIWCSEQLWS AFVLAAVVAL
VICLITFFVV SWILGRQGKQ QSENEVTGGR QLTDNPKDVA RMLKKDGKDS DIRIGDLPII
RDSEIQNFCL HGTVGAGKSE VIRRLANYAR QRGDMVVIYD RSGEFVKSYY DPSIDKILNP
LDARCAAWDL WKECLTQPDF DNTANTLIPM GTKEDPFWQG SGRTIFAEAA YLMRNDPNRS
YSKLVDTLLS IKIEKLRTYL RNSPAANLVE EKIEKTAISI RAVLTNYVKA IRYLQGIEHN
GEPFTIRDWM RGVREDQKNG WLFISSNADT HASLKPVISM WLSIAIRGLL AMGENRNRRV
WFFCDELPTL HKLPDLVEIL PEARKFGGCY VFGIQSYAQL EDIYGEKAAA SLFDVMNTRA
FFRSPSHKIA EFAAGEIGEK EHLKASEQYS YGADPVRDGV STGKDMERQT LVSYSDIQSL
PDLTCYVTLP GPYPAVKLSL KYQTRPKVAP EFIPRDINPE MENRLSAVLA AREAEGRQMA
SLFEPDVPEV VSGEDVTQAE QPQQPVSPAI NDKKSDSGVN VPAGGIEQEL KMKPEEEMEQ
QLPPGISESG EVVDMAAYEA WQQENHPDIQ QQMQRREEVN INVHRERGED VEPGDDF
