ID   TRAQ_ECOLI              Reviewed;          94 AA.
AC   P18033;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Protein TraQ;
GN   Name=traQ; OrderedLocusNames=ECOK12F094;
OS   Escherichia coli (strain K12).
OG   Plasmid F.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2536655; DOI=10.1128/jb.171.1.213-221.1989;
RA   Wu J.H., Ippen-Ihler K.;
RT   "Nucleotide sequence of traQ and adjacent loci in the Escherichia coli K-12
RT   F-plasmid transfer operon.";
RL   J. Bacteriol. 171:213-221(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / CR63;
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   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12; PLASMID=F;
RX   PubMed=1593622; DOI=10.1016/0022-2836(92)90923-8;
RA   Maneewannakul S., Kathir P., Ippen-Ihler K.;
RT   "Characterization of the F plasmid mating aggregation gene traN and of a
RT   new F transfer region locus trbE.";
RL   J. Mol. Biol. 225:299-311(1992).
RN   [5]
RP   INTERACTION WITH PROPILIN.
RC   PLASMID=F;
RX   PubMed=8095257; DOI=10.1128/jb.175.5.1384-1391.1993;
RA   Maneewannakul K., Maneewannakul S., Ippen-Ihler K.;
RT   "Synthesis of F pilin.";
RL   J. Bacteriol. 175:1384-1391(1993).
RN   [6]
RP   FUNCTION IN PROPILIN MATURATION.
RC   PLASMID=F;
RX   PubMed=8730869; DOI=10.1111/j.1365-2958.1996.tb02472.x;
RA   Paiva W.D., Silverman P.M.;
RT   "Effects of F-encoded components and F-pilin domains on the synthesis and
RT   membrane insertion of TraA'-'PhoA fusion proteins.";
RL   Mol. Microbiol. 19:1277-1286(1996).
RN   [7]
RP   INTERACTION WITH PROPILIN.
RC   PLASMID=F;
RX   PubMed=10564517; DOI=10.1046/j.1365-2958.1999.01640.x;
RA   Harris R.L., Sholl K.A., Conrad M.N., Dresser M.E., Silverman P.M.;
RT   "Interaction between the F plasmid TraA (F-pilin) and TraQ proteins.";
RL   Mol. Microbiol. 34:780-791(1999).
CC   -!- FUNCTION: Required for efficient expression of pilin. Functions as a
CC       transient chaperone for propilin, preventing it from being prematurely
CC       degraded, and also promotes propilin translocation, positioning it in
CC       the membrane for processing to mature pilin.
CC       {ECO:0000269|PubMed:8730869}.
CC   -!- SUBUNIT: Interacts with pilin. {ECO:0000269|PubMed:10564517,
CC       ECO:0000269|PubMed:8095257}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:1593622};
CC       Multi-pass membrane protein {ECO:0000305}.
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DR   EMBL; M20787; AAC63070.1; -; Genomic_DNA.
DR   EMBL; U01159; AAC44194.1; -; Genomic_DNA.
DR   EMBL; AP001918; BAA97964.1; -; Genomic_DNA.
DR   PIR; D32238; BVECAQ.
DR   RefSeq; NP_061473.1; NC_002483.1.
DR   RefSeq; NP_862939.1; NC_004998.1.
DR   RefSeq; WP_000624109.1; NZ_CP014273.1.
DR   RefSeq; YP_006953815.1; NC_019089.1.
DR   RefSeq; YP_008826456.1; NC_022885.1.
DR   RefSeq; YP_009066498.1; NC_025106.1.
DR   RefSeq; YP_009068330.1; NC_025139.1.
DR   RefSeq; YP_009070595.1; NC_025175.1.
DR   RefSeq; YP_009071251.1; NC_025179.1.
DR   AlphaFoldDB; P18033; -.
DR   DIP; DIP-27655N; -.
DR   IntAct; P18033; 1.
DR   PRIDE; P18033; -.
DR   PATRIC; fig|83333.107.peg.618; -.
DR   PRO; PR:P18033; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR014112; TraQ.
DR   Pfam; PF09679; TraQ; 1.
DR   PIRSF; PIRSF003265; TraQ; 1.
DR   TIGRFAMs; TIGR02741; TraQ; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Conjugation; Membrane; Plasmid;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..94
FT                   /note="Protein TraQ"
FT                   /id="PRO_0000068475"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   94 AA;  10866 MW;  21132F30801EE31A CRC64;
     MISKRRFSLP RLDITGMWVF SLGVWFHIVA RLVYSKPWMA FFLAELIAAI LVLFGAYQVL
     DAWIARVSRE EREALEARQQ AMMEGQQEGG HVSH