ID   CITB_KLEPN              Reviewed;         234 AA.
AC   P52688;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Transcriptional regulatory protein CitB;
GN   Name=citB;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13882 / NBRC 13541 / NCTC 8172;
RX   PubMed=8748036; DOI=10.1111/j.1365-2958.1995.mmi_18030533.x;
RA   Bott M., Meyer M., Dimroth P.;
RT   "Regulation of anaerobic citrate metabolism in Klebsiella pneumoniae.";
RL   Mol. Microbiol. 18:533-546(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-6, AND CHARACTERIZATION.
RC   STRAIN=ATCC 13882 / NBRC 13541 / NCTC 8172;
RX   PubMed=9223636; DOI=10.1006/jmbi.1997.1076;
RA   Meyer M., Dimroth P., Bott M.;
RT   "In vitro binding of the response regulator CitB and of its carboxy-
RT   terminal domain to A + T-rich DNA target sequences in the control region of
RT   the divergent citC and citS operons of Klebsiella pneumoniae.";
RL   J. Mol. Biol. 269:719-731(1997).
RN   [3]
RP   FUNCTION, PHOSPHORYLATION AT ASP-56, CHARACTERIZATION, AND MUTAGENESIS OF
RP   ASP-56.
RC   STRAIN=ATCC 13882 / NBRC 13541 / NCTC 8172;
RX   PubMed=10447894; DOI=10.1046/j.1365-2958.1999.01536.x;
RA   Kaspar S., Perozzo R., Reinelt S., Meyer M., Pfister K., Scapozza L.,
RA   Bott M.;
RT   "The periplasmic domain of the histidine autokinase CitA functions as a
RT   highly specific citrate receptor.";
RL   Mol. Microbiol. 33:858-872(1999).
CC   -!- FUNCTION: Member of the two-component regulatory system CitA/CitB
CC       essential for expression of citrate-specific fermentation genes.
CC       Phosphorylated CitB binds to two sites in the citS-citC intergenic
CC       region where it probably activates transcription of both genes.
CC       {ECO:0000269|PubMed:10447894}.
CC   -!- SUBUNIT: In vitro CitB and the CitA kinase domain form a complex,
CC       formation of which is enhanced by ATP.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by CitA. {ECO:0000269|PubMed:10447894}.
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DR   EMBL; U31464; AAC44734.1; -; Genomic_DNA.
DR   PIR; S70539; S70539.
DR   RefSeq; WP_004222618.1; NZ_WYAL01000019.1.
DR   AlphaFoldDB; P52688; -.
DR   SMR; P52688; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR024187; Sig_transdc_resp-reg_cit/mal.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR028141; Transcriptional_reg_dom.
DR   PANTHER; PTHR45526; PTHR45526; 1.
DR   Pfam; PF12431; CitT; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF006171; RR_citrat_malat; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW   Phosphoprotein; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           1..234
FT                   /note="Transcriptional regulatory protein CitB"
FT                   /id="PRO_0000081072"
FT   DOMAIN          5..121
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        181..200
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT                   ECO:0000269|PubMed:10447894"
FT   MUTAGEN         56
FT                   /note="D->N: Loss of phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:10447894"
SQ   SEQUENCE   234 AA;  26821 MW;  C793725EE30E3DB8 CRC64;
     MDSITTLIVE DEPMLAEILV DNIKQFPQFD VIGIADKLES ARKQLRLYQP QLILLDNFLP
     DGKGIDLIRH AVSTHYKGRI IFITADNHME TISEALRLGV FDYLIKPVHY QRLQHTLERF
     ARYRSSLRSS EQASQLHVDA LFNIQAREQT EPASAPLRGI DESTFQRVLQ LFADPTVVHT
     ADSLARILGS SKTTARRYLE QGVKNDFLEA EISYGKVGRP ERIYHGKQTY PEQR