ID   TRAN_ECOLI              Reviewed;         602 AA.
AC   P24082;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=Mating pair stabilization protein TraN;
DE   Flags: Precursor;
GN   Name=traN; OrderedLocusNames=ECOK12F089;
OS   Escherichia coli (strain K12).
OG   Plasmid F.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP   AND MUTAGENESIS OF 131-GLN--GLN-602.
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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC   STRAIN=K12;
RX   PubMed=2050638; DOI=10.1128/jb.173.12.3872-3878.1991;
RA   Maneewannakul S., Maneewannakul K., Ippen-Ihler K.;
RT   "Characterization of trbC, a new F plasmid tra operon gene that is
RT   essential to conjugative transfer.";
RL   J. Bacteriol. 173:3872-3878(1991).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-90 AND
RP   584-VAL--GLN-602.
RC   STRAIN=JC3272; PLASMID=F;
RX   PubMed=9696748; DOI=10.1128/jb.180.16.4036-4043.1998;
RA   Klimke W.A., Frost L.S.;
RT   "Genetic analysis of the role of the transfer gene, traN, of the F and
RT   R100-1 plasmids in mating pair stabilization during conjugation.";
RL   J. Bacteriol. 180:4036-4043(1998).
RN   [6]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, PUTATIVE TOPOLOGY,
RP   DISULFIDE BOND, AND MUTAGENESIS OF CYS-147; CYS-478; 501-CYS--CYS-517;
RP   501-CYS--CYS-509; CYS-501; 509-CYS--CYS-517; CYS-509; CYS-517 AND CYS-548.
RC   PLASMID=F;
RX   PubMed=16272376; DOI=10.1099/mic.0.28025-0;
RA   Klimke W.A., Rypien C.D., Klinger B., Kennedy R.A.,
RA   Rodriguez-Maillard J.M., Frost L.S.;
RT   "The mating pair stabilization protein, TraN, of the F plasmid is an outer-
RT   membrane protein with two regions that are important for its function in
RT   conjugation.";
RL   Microbiology 151:3527-3540(2005).
CC   -!- FUNCTION: Essential for F plasmid conjugative transfer. May interact
CC       with the recipient cell surface to stabilize mating pairs initiated by
CC       F-pili. May interact with TraG (Probable). Transfer requires OmpA and
CC       lipopolysaccharide (LPS), which are possibly receptors for TraN
CC       (PubMed:9696748, PubMed:16272376). {ECO:0000269|PubMed:16272376,
CC       ECO:0000269|PubMed:9696748, ECO:0000305|PubMed:1593622}.
CC   -!- SUBUNIT: Interacts with OmpA of recipient cells (Probable)
CC       (PubMed:16272376). Might form multimers (PubMed:16272376). May interact
CC       with TraG (Probable). {ECO:0000269|PubMed:16272376,
CC       ECO:0000305|PubMed:1593622, ECO:0000305|PubMed:9696748}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:1593622,
CC       ECO:0000269|PubMed:16272376}. Note=Part of the protein is accessible to
CC       externally added proteases (PubMed:1593622, PubMed:16272376). A
CC       topology of the protein suggesting it is a beta-barrel has been
CC       proposed; this was not confirmed using bioinformatics programs
CC       available in April 2019 (Probable). {ECO:0000269|PubMed:1593622,
CC       ECO:0000269|PubMed:16272376, ECO:0000305|PubMed:16272376}.
CC   -!- DOMAIN: The first 350 residues are required for recognition of OmpA.
CC       {ECO:0000269|PubMed:16272376}.
CC   -!- PTM: Has higher gel mobility under non-reducing conditions, suggesting
CC       it has disulfide bonds; a dsbA deletion mutant has considerably less
CC       TraN that is still localized in the outer membrane.
CC       {ECO:0000269|PubMed:16272376}.
CC   -!- DISRUPTION PHENOTYPE: Greatly decreased conjugtive transfer.
CC       {ECO:0000269|PubMed:9696748}.
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DR   EMBL; X61575; CAA43775.1; -; Genomic_DNA.
DR   EMBL; U01159; AAC44192.1; -; Genomic_DNA.
DR   EMBL; AP001918; BAA97959.1; -; Genomic_DNA.
DR   EMBL; M60427; AAA24915.1; -; Genomic_DNA.
DR   PIR; S23991; S23991.
DR   RefSeq; NP_061468.1; NC_002483.1.
DR   RefSeq; WP_000821835.1; NZ_JACEFS010000047.1.
DR   AlphaFoldDB; P24082; -.
DR   PATRIC; fig|83333.107.peg.623; -.
DR   OrthoDB; 5297981at2; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR014121; TraN_Ftype.
DR   NCBIfam; TIGR02750; TraN_Ftype; 1.
DR   Pfam; PF06986; F_T4SS_TraN; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Conjugation; Disulfide bond; Membrane; Plasmid;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..602
FT                   /note="Mating pair stabilization protein TraN"
FT                   /id="PRO_0000024508"
FT   MUTAGEN         90
FT                   /note="K->T: 90% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:9696748"
FT   MUTAGEN         131..602
FT                   /note="Missing: In traN548; 0.03% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:1593622"
FT   MUTAGEN         147
FT                   /note="C->S: 1.7% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:16272376"
FT   MUTAGEN         478
FT                   /note="C->S: 1.5% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:16272376"
FT   MUTAGEN         501..517
FT                   /note="CSKKVLGVCLEKKRSYC->SSKKVLGVCLEKKRSYS: 0.3%
FT                   conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:16272376"
FT   MUTAGEN         501..509
FT                   /note="CSKKVLGVC->SSKKVLGVS: 2.3% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:16272376"
FT   MUTAGEN         501
FT                   /note="C->S: 1.7% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:16272376"
FT   MUTAGEN         509..517
FT                   /note="CLEKKRSYC->SLEKKRSYS: 0.004% conjugation
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:16272376"
FT   MUTAGEN         509
FT                   /note="C->S: 5.4% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:16272376"
FT   MUTAGEN         517
FT                   /note="C->S: 0.4% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:16272376"
FT   MUTAGEN         548
FT                   /note="C->S: 0.1% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:16272376"
FT   MUTAGEN         584..602
FT                   /note="Missing: 0.015% conjugation efficiency."
FT                   /evidence="ECO:0000269|PubMed:9696748"
SQ   SEQUENCE   602 AA;  65715 MW;  78B97716681FF50E CRC64;
     MKRILPLILA LVAGMAQADS NSDYRAGSDF AHQIKGQGSS SIQGFKPQES IPGYNANPDE
     TKYYGGVTAG GDGGLKNDGT TEWATGETGK TITESFMNKP KDILSPDAPF IQTGRDVVNR
     ADSIVGNTGQ QCSAQEISRS EYTNYTCERD LQVEQYCTRT ARMELQGSTT WETRTLEYEM
     SQLPAREVNG QYVVSITSPV TGEIVDAHYS WSRTYLQKSV PMTITVLGTP LSWNAKYSAD
     ASFTPVQKTL TAGVAFTSSH PVRVGNTKFK RHTAMKLRLV VRVKKASYTP YVVWSESCPF
     SKELGKLTKT ECTEAGGNRT LVKDGQSYSM YQSCWAYRDT YVTQSADKGT CQTYTDNPAC
     TLVSHQCAFY SEEGACLHEY ATYSCESKTS GKVMVCGGDV FCLDGECDKA QSGKSNDFAE
     AVSQLAALAA AGKDVAALNG VDVRAFTGQA KFCKKAAAGY SNCCKDSGWG QDIGLAKCSS
     DEKALAKAKS NKLTVSVGEF CSKKVLGVCL EKKRSYCQFD SKLAQIVQQQ GRNGQLRISF
     GSAKHPDCRG ITVDELQKIQ FNRLDFTNFY EDLMNNQKIP DSGVLTQKVK EQIADQLKQA
     GQ
//