CHPT_BRUA2
ID CHPT_BRUA2 Reviewed; 209 AA.
AC Q2YQA5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein phosphotransferase ChpT {ECO:0000305|PubMed:26124143};
DE EC=2.7.99.- {ECO:0000305|PubMed:26124143};
DE AltName: Full=Histidine phosphotransferase {ECO:0000303|PubMed:26124143};
GN Name=chpT {ECO:0000303|PubMed:26124143};
GN OrderedLocusNames=BAB1_1613 {ECO:0000312|EMBL:CAJ11569.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH THE
RP RECEIVER DOMAIN OF CTRA, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
RP PHOSPHORYLATION AT HIS-22, INTERACTION WITH CTRA, DISRUPTION PHENOTYPE,
RP DOMAIN, AND MUTAGENESIS OF HIS-22; ASN-33; GLU-36 AND GLU-40.
RC STRAIN=2308;
RX PubMed=26124143; DOI=10.1073/pnas.1503118112;
RA Willett J.W., Herrou J., Briegel A., Rotskoff G., Crosson S.;
RT "Structural asymmetry in a conserved signaling system that regulates
RT division, replication, and virulence of an intracellular pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E3709-E3718(2015).
CC -!- FUNCTION: Component of a regulatory phosphorelay system that controls
CC B.abortus cell growth, division, and intracellular survival inside
CC mammalian host cells. This signaling pathway is composed of CckA, ChpT,
CC CtrA and CpdR. ChpT efficiently and specifically shuttles phosphoryl
CC groups from the CckA kinase to the receiver domains of both CtrA and
CC CpdR. Does not bind ATP. Overexpression of chpT results in a defect in
CC cell morphology, DNA content, and intracellular survival in human
CC macrophages. {ECO:0000269|PubMed:26124143}.
CC -!- SUBUNIT: Homodimer. Forms an asymmetric heterotetramer with CtrA (2:2).
CC There are at least two modes of interaction between ChpT and CtrA, only
CC one of which is competent to catalyze His-Asp phosphoryl transfer.
CC {ECO:0000269|PubMed:26124143}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:26124143}.
CC -!- DOMAIN: Each ChpT monomer is composed of an N-terminal dimerization and
CC histidine phosphotransfer (DHp) domain and a C-terminal domain that is
CC structurally similar to the catalytic and ATP-binding domain found in
CC histidine kinases but that lacks regions required for ATP binding.
CC {ECO:0000269|PubMed:26124143}.
CC -!- PTM: Is phosphorylated by CckA-P on His-22.
CC {ECO:0000269|PubMed:26124143}.
CC -!- DISRUPTION PHENOTYPE: This gene cannot be deleted or disrupted in the
CC absence of a complementary copy expressed in trans, indicating this
CC gene is essential in B.abortus. {ECO:0000269|PubMed:26124143}.
CC -!- SIMILARITY: Belongs to the ChpT phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; AM040264; CAJ11569.1; -; Genomic_DNA.
DR RefSeq; WP_002964698.1; NZ_KN046823.1.
DR PDB; 4QPJ; X-ray; 2.74 A; A/B=1-209.
DR PDB; 4QPK; X-ray; 1.66 A; A/B=1-209.
DR PDBsum; 4QPJ; -.
DR PDBsum; 4QPK; -.
DR AlphaFoldDB; Q2YQA5; -.
DR SMR; Q2YQA5; -.
DR STRING; 359391.BAB1_1613; -.
DR iPTMnet; Q2YQA5; -.
DR EnsemblBacteria; CAJ11569; CAJ11569; BAB1_1613.
DR GeneID; 3788144; -.
DR KEGG; bmf:BAB1_1613; -.
DR PATRIC; fig|359391.11.peg.1063; -.
DR HOGENOM; CLU_086320_0_0_5; -.
DR OMA; KATLKWQ; -.
DR PhylomeDB; Q2YQA5; -.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0018197; P:peptidyl-aspartic acid modification; IDA:UniProtKB.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR018762; ChpT_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR Pfam; PF10090; HPTransfase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kinase; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..209
FT /note="Protein phosphotransferase ChpT"
FT /id="PRO_0000436619"
FT MOD_RES 22
FT /note="Phosphohistidine"
FT /evidence="ECO:0000269|PubMed:26124143"
FT MUTAGEN 22
FT /note="H->A: Loss of phosphoryl transfer from CckA-P to
FT ChpT."
FT /evidence="ECO:0000269|PubMed:26124143"
FT MUTAGEN 33
FT /note="N->R: 5-fold decrease in phosphoryl transfer from
FT CckA-P to ChpT."
FT /evidence="ECO:0000269|PubMed:26124143"
FT MUTAGEN 36
FT /note="E->R: 10-fold decrease in phosphoryl transfer from
FT CckA-P to ChpT."
FT /evidence="ECO:0000269|PubMed:26124143"
FT MUTAGEN 40
FT /note="E->R: 3-fold decrease in phosphoryl transfer from
FT CckA-P to ChpT."
FT /evidence="ECO:0000269|PubMed:26124143"
FT HELIX 9..40
FT /evidence="ECO:0007829|PDB:4QPK"
FT HELIX 44..68
FT /evidence="ECO:0007829|PDB:4QPK"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:4QPK"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:4QPK"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:4QPK"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4QPK"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:4QPK"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:4QPK"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:4QPK"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:4QPK"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4QPK"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:4QPK"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4QPK"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4QPK"
SQ SEQUENCE 209 AA; 22279 MW; E495DC3E52030BC5 CRC64;
MSLPVTLSAL DLGALLCSRI CHDIISPVGA INNGLELLEE GGADEDAMAL IKSSARNASA
RLQFARIAFG AAGSAGVQID TGDAQNVATE YFRNEKPEFT WEGARVLLPK NKVKLLLNML
LIGNGAIPRG GSLAVRLEGS DTDPRFVITV KGRMLRVPPK FLELHSGAAP EEPIDAHSVQ
PYYTLLLAEE AGMKISIHAT AEDIVFSAE
