FINO3_ECOLX
ID FINO3_ECOLX Reviewed; 186 AA.
AC P29367;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Fertility inhibition protein;
DE AltName: Full=Conjugal transfer repressor;
GN Name=finO;
OS Escherichia coli.
OG Plasmid R6-5.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1916281; DOI=10.1016/0378-1119(91)90469-r;
RA Cram D.S., Loh S.M., Cheah K.C., Skurray R.A.;
RT "Sequence and conservation of genes at the distal end of the transfer
RT region on plasmids F and R6-5.";
RL Gene 104:85-90(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10876242; DOI=10.1038/76790;
RA Ghetu A.F., Gubbins M.J., Frost L.S., Glover J.N.;
RT "Crystal structure of the bacterial conjugation repressor finO.";
RL Nat. Struct. Biol. 7:565-569(2000).
CC -!- FUNCTION: One of the components on the FinOP fertility inhibition
CC complex, which inhibits the expression of traJ gene, which in turn
CC regulates the expression of some 20 transfer genes. The transfer genes
CC are responsible for the process, called conjugal transfer, in which DNA
CC is transmitted from one bacterial host to another. RNA-binding that
CC interacts with the traJ mRNA and its antisense RNA, finP, stabilizing
CC finP against endonucleolytic degradation and facilitating sense-
CC antisense RNA recognition (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FinO family. {ECO:0000305}.
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DR EMBL; M38048; AAA98316.1; -; Genomic_DNA.
DR RefSeq; WP_000139323.1; NZ_WSWZ01000049.1.
DR RefSeq; YP_002456228.1; NC_011812.1.
DR RefSeq; YP_006952274.1; NC_019057.1.
DR RefSeq; YP_006953358.1; NC_019071.1.
DR RefSeq; YP_006953456.1; NC_019072.1.
DR RefSeq; YP_006953983.1; NC_019090.1.
DR RefSeq; YP_006954301.1; NC_019095.1.
DR RefSeq; YP_007447581.1; NC_020278.2.
DR PDB; 1DVO; X-ray; 2.00 A; A=33-184.
DR PDBsum; 1DVO; -.
DR AlphaFoldDB; P29367; -.
DR SMR; P29367; -.
DR EvolutionaryTrace; P29367; -.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1710.10; -; 1.
DR InterPro; IPR021065; Fertility_inhibition_FinO_N.
DR InterPro; IPR016103; ProQ/FinO.
DR InterPro; IPR036442; ProQ/FinO_sf.
DR Pfam; PF12602; FinO_N; 1.
DR Pfam; PF04352; ProQ; 1.
DR SMART; SM00945; ProQ; 1.
DR SUPFAM; SSF48657; SSF48657; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Conjugation; Plasmid; Repressor; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..186
FT /note="Fertility inhibition protein"
FT /id="PRO_0000068352"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 35..64
FT /evidence="ECO:0007829|PDB:1DVO"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1DVO"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:1DVO"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1DVO"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1DVO"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:1DVO"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:1DVO"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:1DVO"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1DVO"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1DVO"
FT HELIX 156..183
FT /evidence="ECO:0007829|PDB:1DVO"
SQ SEQUENCE 186 AA; 21280 MW; D263B2BE06E2805D CRC64;
MTEQKRPVLT LKRKTEGETP TRSRKTIINV TTPPKWKVKK QKLAEKAARE AELTAKKAQA
RQALSIYLNL PTLDEAVNTL KPWWPGLFDG DTPRLLACGI RDVLLEDVAQ RNIPLSHKKL
RRALKAITRS ESYLCAMKAG ACRYDTEGYV TEHISQEEEV YAAERLDKIR RQNRIKAELQ
AVLDEQ