TRAN_ECOLI
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 03-AUG-2022, entry version 102.
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; Proteobacteria; 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_CP014273.1.
DR AlphaFoldDB; P24082; -.
DR PRIDE; P24082; -.
DR PATRIC; fig|83333.107.peg.623; -.
DR PRO; PR:P24082; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR014121; TraN_Ftype.
DR Pfam; PF06986; TraN; 1.
DR TIGRFAMs; TIGR02750; TraN_Ftype; 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
