CHXR_CHLT2
ID CHXR_CHLT2 Reviewed; 227 AA.
AC A0A0H3MDW1;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Atypical response regulator protein ChxR {ECO:0000303|PubMed:21775428};
DE AltName: Full=Transcriptional regulatory protein {ECO:0000312|EMBL:CAP04331.1};
GN Name=chxR {ECO:0000303|PubMed:21057008};
GN OrderedLocusNames=CTL0894 {ECO:0000312|EMBL:CAP04331.1};
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472 {ECO:0000312|EMBL:CAP04331.1};
RN [1] {ECO:0000312|EMBL:CAP04331.1, ECO:0000312|Proteomes:UP000000795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B {ECO:0000312|Proteomes:UP000000795};
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
RN [2]
RP FUNCTION, DNA-BINDING, SUBUNIT, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP GLU-49.
RC STRAIN=434/Bu / ATCC VR-902B {ECO:0000303|PubMed:21057008};
RX PubMed=21057008; DOI=10.1128/jb.00833-10;
RA Hickey J.M., Weldon L., Hefty P.S.;
RT "The atypical OmpR/PhoB response regulator ChxR from Chlamydia trachomatis
RT forms homodimers in vivo and binds a direct repeat of nucleotide
RT sequences.";
RL J. Bacteriol. 193:389-398(2011).
RN [3] {ECO:0007744|PDB:3Q7R, ECO:0007744|PDB:3Q7S, ECO:0007744|PDB:3Q7T}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-113, FUNCTION, DNA-BINDING,
RP SUBUNIT, CIRCULAR DICHROISM ANALYSIS, AND MUTAGENESIS OF GLU-49; ASP-73;
RP GLU-78; TRP-89 AND LYS-101.
RC STRAIN=434/Bu / ATCC VR-902B {ECO:0000303|PubMed:21775428};
RX PubMed=21775428; DOI=10.1074/jbc.m111.220574;
RA Hickey J.M., Lovell S., Battaile K.P., Hu L., Middaugh C.R., Hefty P.S.;
RT "The atypical response regulator protein ChxR has structural
RT characteristics and dimer interface interactions that are unique within the
RT OmpR/PhoB subfamily.";
RL J. Biol. Chem. 286:32606-32616(2011).
RN [4] {ECO:0007744|PDB:2M1B}
RP STRUCTURE BY NMR OF 114-227, FUNCTION, DNA-BINDING, SUBUNIT, AND
RP MUTAGENESIS OF ASN-182; ASP-184; HIS-186; ILE-187; ARG-191; LYS-192;
RP ARG-205 AND VAL-207.
RC STRAIN=434/Bu / ATCC VR-902B {ECO:0000303|PubMed:24646934};
RX PubMed=24646934; DOI=10.1371/journal.pone.0091760;
RA Barta M.L., Hickey J.M., Anbanandam A., Dyer K., Hammel M., Hefty P.S.;
RT "Atypical response regulator ChxR from Chlamydia trachomatis is
RT structurally poised for DNA binding.";
RL PLoS ONE 9:E91760-E91760(2014).
CC -!- FUNCTION: May be a global positive regulator of transcription
CC (PubMed:21057008). Binds a cis-acting element of its own promoter DNA
CC sequence and is hence probably also involved in its own transcription
CC activation (PubMed:21057008, PubMed:21775428, PubMed:24646934). The
CC recognition sequence is 5'-WHGAWNH-N(3-5)-WHGAWNH-3', where W is A/T, H
CC is C/A/T, N is G/C/A/T and the linker length in the middle is 3 to 5
CC nucleotides (PubMed:21057008). {ECO:0000269|PubMed:21057008,
CC ECO:0000269|PubMed:21775428, ECO:0000269|PubMed:24646934}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21057008,
CC ECO:0000269|PubMed:21775428, ECO:0000269|PubMed:24646934}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the middle and late stages of the
CC chlamydial developmental cycle including the stage of the formation of
CC infectious elementary bodies. {ECO:0000269|PubMed:21057008}.
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DR EMBL; AM884176; CAP04331.1; -; Genomic_DNA.
DR RefSeq; WP_009873961.1; NC_010287.1.
DR RefSeq; YP_001654963.1; NC_010287.1.
DR PDB; 2M1B; NMR; -; A=114-227.
DR PDB; 3Q7R; X-ray; 1.60 A; A/B=2-113.
DR PDB; 3Q7S; X-ray; 2.10 A; A/B=2-113.
DR PDB; 3Q7T; X-ray; 2.15 A; A/B=2-113.
DR PDBsum; 2M1B; -.
DR PDBsum; 3Q7R; -.
DR PDBsum; 3Q7S; -.
DR PDBsum; 3Q7T; -.
DR AlphaFoldDB; A0A0H3MDW1; -.
DR BMRB; A0A0H3MDW1; -.
DR SMR; A0A0H3MDW1; -.
DR EnsemblBacteria; CAP04331; CAP04331; CTL0894.
DR KEGG; ctb:CTL0894; -.
DR PATRIC; fig|471472.4.peg.960; -.
DR HOGENOM; CLU_1265073_0_0_0; -.
DR OMA; AIFCEYL; -.
DR PHI-base; PHI:7471; -.
DR Proteomes; UP000000795; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..227
FT /note="Atypical response regulator protein ChxR"
FT /id="PRO_0000433386"
FT DOMAIN 6..108
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 117..213
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MUTAGEN 49
FT /note="E->A: No effect on DNA-binding or dimerization. No
FT effect on DNA-binding or dimerization; when associated with
FT A-73."
FT /evidence="ECO:0000269|PubMed:21775428"
FT MUTAGEN 49
FT /note="E->D: No effect on DNA-binding or dimerization."
FT /evidence="ECO:0000269|PubMed:21057008"
FT MUTAGEN 73
FT /note="D->A: No effect on DNA-binding or dimerization. No
FT effect on DNA-binding or dimerization; when associated with
FT A-49."
FT /evidence="ECO:0000269|PubMed:21775428"
FT MUTAGEN 78
FT /note="E->A: No effect on DNA-binding or dimerization. No
FT effect on DNA-binding or dimerization; when associated with
FT A-101."
FT /evidence="ECO:0000269|PubMed:21775428"
FT MUTAGEN 89
FT /note="W->A: No effect on DNA-binding or dimerization."
FT /evidence="ECO:0000269|PubMed:21775428"
FT MUTAGEN 89
FT /note="W->E: Significantly reduced DNA-binding. No
FT dimerization."
FT /evidence="ECO:0000269|PubMed:21775428"
FT MUTAGEN 101
FT /note="K->A: No effect on DNA-binding or dimerization. No
FT effect on DNA-binding or dimerization; when associated with
FT A-78."
FT /evidence="ECO:0000269|PubMed:21775428"
FT MUTAGEN 182
FT /note="N->A: Significantly reduced DNA-binding."
FT /evidence="ECO:0000269|PubMed:24646934"
FT MUTAGEN 184
FT /note="D->A: No effect on DNA-binding."
FT /evidence="ECO:0000269|PubMed:24646934"
FT MUTAGEN 186
FT /note="H->A: Significantly reduced DNA-binding."
FT /evidence="ECO:0000269|PubMed:24646934"
FT MUTAGEN 187
FT /note="I->A: No effect on DNA-binding."
FT /evidence="ECO:0000269|PubMed:24646934"
FT MUTAGEN 191
FT /note="R->A: Protein localization in inclusion bodies."
FT /evidence="ECO:0000269|PubMed:24646934"
FT MUTAGEN 192
FT /note="K->A: Significantly reduced DNA-binding."
FT /evidence="ECO:0000269|PubMed:24646934"
FT MUTAGEN 205
FT /note="R->A: Significantly reduced DNA-binding."
FT /evidence="ECO:0000269|PubMed:24646934"
FT MUTAGEN 207
FT /note="V->A: No effect on DNA-binding."
FT /evidence="ECO:0000269|PubMed:24646934"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:3Q7R"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:3Q7R"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3Q7R"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3Q7R"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:3Q7R"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3Q7R"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3Q7R"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:3Q7R"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3Q7R"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:3Q7R"
SQ SEQUENCE 227 AA; 25835 MW; D593556F74B5B2E8 CRC64;
MAGPKHVLLV SEHWDLFFQT KELLNPEEYR CTIGQQYKQE LSADLVVCEY SLLPREIRSP
KSLEGSFVLV LLDFFDEETS VDLLDRGFWY LIRPITPRIL KSAISLFLSQ HSLHSVPESI
RFGPNVFYVL KLTVETPEGS VHLTPSESGI LKRLLINKGQ LCLRKHLLEE IKNHAKAIVA
RNVDVHIASL RKKLGAYGSR IVTLRGVGYL FSDDGDKKFS QQDTKLS
