IHFB_ECOLI
ID IHFB_ECOLI Reviewed; 94 AA.
AC P0A6Y1; P08756;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Integration host factor subunit beta;
DE Short=IHF-beta;
GN Name=ihfB; Synonyms=himD, hip; OrderedLocusNames=b0912, JW0895;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3159903; DOI=10.1016/0022-2836(85)90206-2;
RA Flamm E., Weisberg R.A.;
RT "Primary structure of the hip gene of Escherichia coli and of its product,
RT the beta subunit of integration host factor.";
RL J. Mol. Biol. 183:117-128(1985).
RN [2]
RP SEQUENCE REVISION TO 90.
RX PubMed=1917861; DOI=10.1128/jb.173.19.6297-6299.1991;
RA Haluzi H., Goitein D., Koby S., Mendelson I., Teff D., Mengeritsky G.,
RA Giladi H., Oppenheim A.B.;
RT "Genes coding for integration host factor are conserved in Gram-negative
RT bacteria.";
RL J. Bacteriol. 173:6297-6299(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-10.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [7]
RP MUTAGENESIS.
RX PubMed=1531459; DOI=10.1002/j.1460-2075.1992.tb05053.x;
RA Lee E.C., Hales L.M., Gumport R.I., Gardner J.F.;
RT "The isolation and characterization of mutants of the integration host
RT factor (IHF) of Escherichia coli with altered, expanded DNA-binding
RT specificities.";
RL EMBO J. 11:305-313(1992).
RN [8]
RP FUNCTION IN CONJUGATION, AND FUNCTION IN F PLASMID NICKING.
RX PubMed=7499339; DOI=10.1074/jbc.270.47.28381;
RA Nelson W.C., Howard M.T., Sherman J.A., Matson S.W.;
RT "The traY gene product and integration host factor stimulate Escherichia
RT coli DNA helicase I-catalyzed nicking at the F plasmid oriT.";
RL J. Biol. Chem. 270:28374-28380(1995).
RN [9]
RP CHARACTERIZATION OF RELAXOSOME ASSEMBLY ORDER, AND SUBUNIT.
RX PubMed=7499340; DOI=10.1074/jbc.270.47.28374;
RA Howard M.T., Nelson W.C., Matson S.W.;
RT "Stepwise assembly of a relaxosome at the F plasmid origin of transfer.";
RL J. Biol. Chem. 270:28381-28386(1995).
RN [10]
RP FUNCTION IN CONJUGATION, DNA-BINDING, AND SUBUNIT.
RX PubMed=17238924; DOI=10.1111/j.1365-2958.2006.05576.x;
RA Ragonese H., Haisch D., Villareal E., Choi J.H., Matson S.W.;
RT "The F plasmid-encoded TraM protein stimulates relaxosome-mediated cleavage
RT at oriT through an interaction with TraI.";
RL Mol. Microbiol. 63:1173-1184(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8980235; DOI=10.1016/s0092-8674(00)81824-3;
RA Rice P.A., Yang S., Mizuuchi K., Nash H.A.;
RT "Crystal structure of an IHF-DNA complex: a protein-induced DNA U-turn.";
RL Cell 87:1295-1306(1996).
CC -!- FUNCTION: One of the 2 subunits of integration host factor (IHF), a
CC specific DNA-binding protein that functions in genetic recombination as
CC well as in transcriptional and translational control.
CC -!- FUNCTION: Plays a crucial role in the lysogenic life cycle of
CC bacteriophage lambda, as it is required not only in the recombination
CC reaction, which inserts lambda DNA into the E.coli chromosome, but also
CC for the synthesis of int and cI repressor, two phage proteins necessary
CC for DNA insertion and repression, respectively. The synthesis of int
CC and cI proteins is regulated indirectly by IHF via translational
CC control of the lambda cII protein.
CC -!- FUNCTION: Has an essential role in conjugative DNA transfer (CDT), the
CC unidirectional transfer of ssDNA plasmid from a donor to a recipient
CC cell. It is the central mechanism by which antibiotic resistance and
CC virulence factors are propagated in bacterial populations. Part of the
CC relaxosome, which facilitates a site- and strand-specific cut in the
CC origin of transfer by TraI, at the nic site. Relaxosome formation
CC requires binding of IHF and TraY to the oriT region, which then
CC facilitates binding of TraI.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. Part of the
CC relaxosome, a complex composed of plasmid-encoded TraI, TraM, TraY and
CC host-encoded IHF bound to the F plasmid origin of transfer (oriT).
CC {ECO:0000269|PubMed:17238924, ECO:0000269|PubMed:7499340}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
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DR EMBL; X04864; CAA28557.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73998.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35656.1; -; Genomic_DNA.
DR PIR; G64830; IQECAB.
DR RefSeq; NP_415432.1; NC_000913.3.
DR RefSeq; WP_000167336.1; NZ_STEB01000006.1.
DR PDB; 1IHF; X-ray; 2.20 A; B=1-94.
DR PDB; 1OUZ; X-ray; 2.41 A; B=1-94.
DR PDB; 1OWF; X-ray; 1.95 A; B=1-94.
DR PDB; 1OWG; X-ray; 2.10 A; B=1-94.
DR PDB; 2HT0; X-ray; 2.00 A; B=1-94.
DR PDB; 2IIE; X-ray; 2.41 A; A=2-94.
DR PDB; 2IIF; X-ray; 2.72 A; A=2-94.
DR PDB; 5J0N; EM; 11.00 A; J/L=1-94.
DR PDBsum; 1IHF; -.
DR PDBsum; 1OUZ; -.
DR PDBsum; 1OWF; -.
DR PDBsum; 1OWG; -.
DR PDBsum; 2HT0; -.
DR PDBsum; 2IIE; -.
DR PDBsum; 2IIF; -.
DR PDBsum; 5J0N; -.
DR AlphaFoldDB; P0A6Y1; -.
DR SMR; P0A6Y1; -.
DR BioGRID; 4263061; 195.
DR ComplexPortal; CPX-1957; Integration host factor complex.
DR DIP; DIP-41099N; -.
DR IntAct; P0A6Y1; 34.
DR STRING; 511145.b0912; -.
DR jPOST; P0A6Y1; -.
DR PaxDb; P0A6Y1; -.
DR PRIDE; P0A6Y1; -.
DR EnsemblBacteria; AAC73998; AAC73998; b0912.
DR EnsemblBacteria; BAA35656; BAA35656; BAA35656.
DR GeneID; 67414200; -.
DR GeneID; 945533; -.
DR KEGG; ecj:JW0895; -.
DR KEGG; eco:b0912; -.
DR PATRIC; fig|1411691.4.peg.1364; -.
DR EchoBASE; EB0436; -.
DR eggNOG; COG0776; Bacteria.
DR HOGENOM; CLU_105066_2_0_6; -.
DR InParanoid; P0A6Y1; -.
DR OMA; RDRVNIY; -.
DR PhylomeDB; P0A6Y1; -.
DR BioCyc; EcoCyc:PD00348; -.
DR EvolutionaryTrace; P0A6Y1; -.
DR PRO; PR:P0A6Y1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990177; C:IHF-DNA complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0006417; P:regulation of translation; IC:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR Gene3D; 4.10.520.10; -; 1.
DR HAMAP; MF_00381; IHF_beta; 1.
DR InterPro; IPR000119; Hist_DNA-bd.
DR InterPro; IPR020816; Histone-like_DNA-bd_CS.
DR InterPro; IPR010992; IHF-like_DNA-bd_dom_sf.
DR InterPro; IPR005685; IHF_beta.
DR PANTHER; PTHR33175; PTHR33175; 1.
DR Pfam; PF00216; Bac_DNA_binding; 1.
DR PRINTS; PR01727; DNABINDINGHU.
DR SMART; SM00411; BHL; 1.
DR SUPFAM; SSF47729; SSF47729; 1.
DR TIGRFAMs; TIGR00988; hip; 1.
DR PROSITE; PS00045; HISTONE_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Conjugation; Cytoplasm; Direct protein sequencing;
KW DNA recombination; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..94
FT /note="Integration host factor subunit beta"
FT /id="PRO_0000105048"
FT MUTAGEN 44
FT /note="E->G,K,V: Altered DNA-binding specificity."
FT /evidence="ECO:0000269|PubMed:1531459"
FT CONFLICT 9
FT /note="R -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1OWF"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1OWG"
FT HELIX 19..38
FT /evidence="ECO:0007829|PDB:1OWF"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1OWF"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1OWF"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1OWF"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1OWF"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1OWF"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1OWF"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1OWF"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:1OWF"
SQ SEQUENCE 94 AA; 10651 MW; 7558D89EF469EA26 CRC64;
MTKSELIERL ATQQSHIPAK TVEDAVKEML EHMASTLAQG ERIEIRGFGS FSLHYRAPRT
GRNPKTGDKV ELEGKYVPHF KPGKELRDRA NIYG
