KORB2_ECOLX
ID KORB2_ECOLX Reviewed; 358 AA.
AC P07674;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Transcriptional repressor protein KorB;
GN Name=korB;
OS Escherichia coli.
OG Plasmid IncP-alpha RK2.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3309894; DOI=10.1093/nar/15.18.7443;
RA Theophilus B.D.B., Thomas C.M.;
RT "Nucleotide sequence of the transcriptional repressor gene korB which plays
RT a key role in regulation of the copy number of broad host range plasmid
RT RK2.";
RL Nucleic Acids Res. 15:7443-7450(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3430606; DOI=10.1016/0022-2836(87)90307-x;
RA Kornacki J.A., Balderes P.J., Figurski D.H.;
RT "Nucleotide sequence of korB, a replication control gene of broad host-
RT range plasmid RK2.";
RL J. Mol. Biol. 198:211-222(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
RX PubMed=3520485; DOI=10.1093/nar/14.11.4453;
RA Thomas C.M., Smith C.A.;
RT "The trfB region of broad host range plasmid RK2: the nucleotide sequence
RT reveals incC and key regulatory gene trfB/korA/korD as overlapping genes.";
RL Nucleic Acids Res. 14:4453-4469(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 327-358.
RX PubMed=1987165; DOI=10.1128/jb.173.2.826-833.1991;
RA Jagura-Burdzy G., Ibbotson J.P., Thomas C.M.;
RT "The korF region of broad-host-range plasmid RK2 encodes two polypeptides
RT with transcriptional repressor activity.";
RL J. Bacteriol. 173:826-833(1991).
CC -!- FUNCTION: In conjunction with KorA, inhibits the transcription of the
CC kilA, trfA and korAB operons. Is also involved in the negative control
CC of the kilB operon.
CC -!- INTERACTION:
CC P07674; P03052: trfB; NbExp=2; IntAct=EBI-6405482, EBI-6405477;
CC -!- SIMILARITY: Belongs to the ParB family. {ECO:0000305}.
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DR EMBL; Y00448; CAA68503.1; -; Genomic_DNA.
DR EMBL; X03962; CAA27598.1; -; Genomic_DNA.
DR EMBL; X06543; CAA29790.1; -; Genomic_DNA.
DR PIR; A26837; RPECKB.
DR RefSeq; WP_011205828.1; NZ_NJTR01000055.1.
DR PDB; 1IGQ; X-ray; 1.70 A; A/B/C/D=297-358.
DR PDB; 1IGU; X-ray; 2.20 A; A/B=297-358.
DR PDB; 1R71; X-ray; 2.20 A; A/B/C/D=117-294.
DR PDBsum; 1IGQ; -.
DR PDBsum; 1IGU; -.
DR PDBsum; 1R71; -.
DR AlphaFoldDB; P07674; -.
DR SMR; P07674; -.
DR DIP; DIP-17007N; -.
DR IntAct; P07674; 1.
DR EvolutionaryTrace; P07674; -.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IMP:CAFA.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR DisProt; DP00656; -.
DR Gene3D; 1.10.10.730; -; 1.
DR Gene3D; 2.30.30.150; -; 1.
DR InterPro; IPR010575; KorB_C.
DR InterPro; IPR037048; KorB_C_sf.
DR InterPro; IPR042075; KorB_DNA-db.
DR InterPro; IPR013741; KorB_domain.
DR InterPro; IPR004437; ParB/RepB/Spo0J.
DR InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR InterPro; IPR008988; Transcriptional_repressor_C.
DR Pfam; PF08535; KorB; 1.
DR Pfam; PF06613; KorB_C; 1.
DR Pfam; PF02195; ParBc; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; SSF110849; 1.
DR SUPFAM; SSF50037; SSF50037; 1.
DR TIGRFAMs; TIGR00180; parB_part; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Plasmid; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..358
FT /note="Transcriptional repressor protein KorB"
FT /id="PRO_0000178699"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:1R71"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:1R71"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:1R71"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:1R71"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1R71"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:1R71"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:1R71"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:1R71"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:1R71"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:1IGQ"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:1IGQ"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:1IGQ"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:1IGQ"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:1IGQ"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:1IGQ"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:1IGQ"
SQ SEQUENCE 358 AA; 39011 MW; 52F49477363F2279 CRC64;
MTAAQAKTTK KNTAAAAQEA AGAAQPSGLG LDSIGDLSSL LDAPAASQGG SGPIELDLDL
IDEDPHQPRT ADNPGFSPES IAEIGATIKE RGVKSPISVR ENQEQPGRYI INHGARRYRG
SKWAGKKSIP AFIDNDYNEA DQVIENLQRN ELTPREIADF IGRELAKGKK KGDIAKEIGK
SPAFITQHVT LLDLPEKIAD AFNTGRVRDV TVVNELVTAF KKRPEEVEAW LDDDTQEITR
GTVKLLREFL DEKGRDPNTV DAFNGQTDAE RDAEAGDGQD GEDGDQDGKD AKEKGAKEPD
PDKLKKAIVQ VEHDERPARL ILNRRPPAEG YAWLKYEDDG QEFEANLADV KLVALIEG
