DPIB_ECOLI
ID DPIB_ECOLI Reviewed; 552 AA.
AC P77510; O54338;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Sensor histidine kinase DpiB;
DE EC=2.7.13.3;
DE AltName: Full=Sensor histidine kinase CitA;
GN Name=dpiB; Synonyms=citA, mpdB, ybeP; OrderedLocusNames=b0619, JW0611;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9701802; DOI=10.1046/j.1365-2958.1998.00895.x;
RA Ingmer H., Miller C.A., Cohen S.N.;
RT "Destabilized inheritance of pSC101 and other Escherichia coli plasmids by
RT DpiA, a novel two-component system regulator.";
RL Mol. Microbiol. 29:49-59(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, CITRATE-BINDING, DOMAIN, AND MUTAGENESIS OF GLY-138.
RX PubMed=11889485; DOI=10.1007/s00203-001-0393-z;
RA Kaspar S., Bott M.;
RT "The sensor kinase CitA (DpiB) of Escherichia coli functions as a high-
RT affinity citrate receptor.";
RL Arch. Microbiol. 177:313-321(2002).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, DOMAIN, AUTOPHOSPHORYLATION, AND MUTAGENESIS
RP OF CYS-478; CYS-517 AND CYS-529.
RX PubMed=19202292; DOI=10.1271/bbb.80586;
RA Yamamoto K., Matsumoto F., Minagawa S., Oshima T., Fujita N., Ogasawara N.,
RA Ishihama A.;
RT "Characterization of CitA-CitB signal transduction activating genes
RT involved in anaerobic citrate catabolism in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 73:346-350(2009).
CC -!- FUNCTION: Member of the two-component regulatory system DpiA/DpiB,
CC which is essential for expression of citrate-specific fermentation
CC genes and genes involved in plasmid inheritance. Could be involved in
CC response to both the presence of citrate and external redox conditions.
CC Functions as a sensor kinase that phosphorylates DpiA in the presence
CC of citrate. {ECO:0000269|PubMed:11889485, ECO:0000269|PubMed:19202292}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- ACTIVITY REGULATION: Autophosphorylation is induced in vitro by
CC dithiothreitol (DTT). {ECO:0000269|PubMed:19202292}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- DOMAIN: The periplasmic domain binds citrate with high affinity. The C-
CC terminal cytoplasmic domain senses reduced conditions using a single
CC Cys in vitro. {ECO:0000269|PubMed:11889485,
CC ECO:0000269|PubMed:19202292}.
CC -!- PTM: Autophosphorylated.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U46667; AAC28951.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40819.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73720.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35255.1; -; Genomic_DNA.
DR PIR; A64796; A64796.
DR RefSeq; NP_415152.1; NC_000913.3.
DR RefSeq; WP_000939767.1; NZ_SSZK01000032.1.
DR AlphaFoldDB; P77510; -.
DR SMR; P77510; -.
DR BioGRID; 4263372; 14.
DR IntAct; P77510; 6.
DR STRING; 511145.b0619; -.
DR PaxDb; P77510; -.
DR PRIDE; P77510; -.
DR EnsemblBacteria; AAC73720; AAC73720; b0619.
DR EnsemblBacteria; BAA35255; BAA35255; BAA35255.
DR GeneID; 945233; -.
DR KEGG; ecj:JW0611; -.
DR KEGG; eco:b0619; -.
DR PATRIC; fig|511145.12.peg.649; -.
DR EchoBASE; EB3410; -.
DR eggNOG; COG3290; Bacteria.
DR HOGENOM; CLU_020211_11_2_6; -.
DR OMA; HIESNYV; -.
DR PhylomeDB; P77510; -.
DR BioCyc; EcoCyc:G6345-MON; -.
DR BioCyc; MetaCyc:G6345-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P77510; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; ISM:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF103190; SSF103190; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF55890; SSF55890; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..552
FT /note="Sensor histidine kinase DpiB"
FT /id="PRO_0000074732"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..182
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 222..292
FT /note="PAS"
FT DOMAIN 344..541
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 347
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MUTAGEN 138
FT /note="G->R: Reduces strongly citrate binding."
FT /evidence="ECO:0000269|PubMed:11889485"
FT MUTAGEN 478
FT /note="C->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19202292"
FT MUTAGEN 517
FT /note="C->A: Decrease in autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19202292"
FT MUTAGEN 529
FT /note="C->A: Constitutively active."
FT /evidence="ECO:0000269|PubMed:19202292"
FT CONFLICT 518..552
FT /note="GGVITLEDNDPCGTLFSIYIPKVKPNDSSINPIDR -> VVLSLSKIMIPAV
FT PYFQSIFRK (in Ref. 1; AAC28951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 61684 MW; 3E3F0E081ABD6E77 CRC64;
MLQLNENKQF AFFQRLAFPL RIFLLILVFS IFVIAALAQY FTASFEDYLT LHVRDMAMNQ
AKIIASNDSV ISAVKTRDYK RLATIANKLQ RDTDFDYVVI GDRHSIRLYH PNPEKIGYPM
QFTKQGALEK GESYFITGKG SMGMAMRAKT PIFDDDGKVI GVVSIGYLVS KIDSWRAEFL
LPMAGVFVVL LGILMLLSWF LAAHIRRQMM GMEPKQIARV VRQQEALFSS VYEGLIAVDP
HGYITAINRN ARKMLGLSSP GRQWLGKPIV EVVRPADFFT EQIDEKRQDV VANFNGLSVI
ANREAIRSGD DLLGAIISFR SKDEISTLNA QLTQIKQYVE SLRTLRHEHL NWMSTLNGLL
QMKEYDRVLA MVQGESQAQQ QLIDSLREAF ADRQVAGLLF GKVQRARELG LKMIIVPGSQ
LSQLPPGLDS TEFAAIVGNL LDNAFEASLR SDEGNKIVEL FLSDEGDDVV IEVADQGCGV
PESLRDKIFE QGVSTRADEP GEHGIGLYLI ASYVTRCGGV ITLEDNDPCG TLFSIYIPKV
KPNDSSINPI DR
