CITA_KLEPN
ID CITA_KLEPN Reviewed; 547 AA.
AC P52687;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sensor histidine kinase CitA;
DE EC=2.7.13.3;
GN Name=citA;
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 FUNCTION, CITRATE-BINDING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION,
RP CHARACTERIZATION, AND MUTAGENESIS OF HIS-350.
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).
RN [3]
RP MUTAGENESIS OF ARG-109; HIS-112; ARG-141; ARG-150 AND LYS-152.
RX PubMed=12741850; DOI=10.1021/bi0340595;
RA Gerharz T., Reinelt S., Kaspar S., Scapozza L., Bott M.;
RT "Identification of basic amino acid residues important for citrate binding
RT by the periplasmic receptor domain of the sensor kinase CitA.";
RL Biochemistry 42:5917-5924(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH CITRATE.
RX PubMed=12867417; DOI=10.1074/jbc.m305864200;
RA Reinelt S., Hofmann E., Gerharz T., Bott M., Madden D.R.;
RT "The structure of the periplasmic ligand-binding domain of the sensor
RT kinase CitA reveals the first extracellular PAS domain.";
RL J. Biol. Chem. 278:39189-39196(2003).
CC -!- FUNCTION: Member of the two-component regulatory system CitA/CitB.
CC Probably activates CitB by phosphorylation. The periplasmic domain
CC binds H-citrate(2-), which is essential for induction of the citrate-
CC fermentation genes. {ECO:0000269|PubMed:10447894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:10447894};
CC -!- SUBUNIT: Homodimer. In vitro CitB and the CitA kinase domain form a
CC complex, formation of which is enhanced by ATP.
CC {ECO:0000269|PubMed:12867417}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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; U31464; AAC44733.1; -; Genomic_DNA.
DR PIR; S70538; S70538.
DR PDB; 1P0Z; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J=48-176.
DR PDB; 2J80; X-ray; 1.60 A; A/B=45-176.
DR PDB; 2V9A; X-ray; 2.00 A; A/B=45-176.
DR PDB; 6LNP; X-ray; 2.99 A; B/D=47-179.
DR PDBsum; 1P0Z; -.
DR PDBsum; 2J80; -.
DR PDBsum; 2V9A; -.
DR PDBsum; 6LNP; -.
DR AlphaFoldDB; P52687; -.
DR SMR; P52687; -.
DR DrugBank; DB04494; Dihydroxy(oxo)molybdenum(6+).
DR DrugBank; DB04414; Heptamolybdate.
DR BRENDA; 2.7.13.3; 2814.
DR EvolutionaryTrace; P52687; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:UniProt.
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; 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; PF17203; sCache_3_2; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 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 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..547
FT /note="Sensor histidine kinase CitA"
FT /id="PRO_0000074733"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..180
FT /note="Periplasmic"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 225..264
FT /note="PAS"
FT DOMAIN 347..542
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 109
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000269|PubMed:12867417"
FT BINDING 112
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000269|PubMed:12867417"
FT BINDING 150
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000269|PubMed:12867417"
FT BINDING 152
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000269|PubMed:12867417"
FT MOD_RES 350
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000305"
FT MUTAGEN 109
FT /note="R->A: Reduces strongly citrate binding."
FT /evidence="ECO:0000269|PubMed:12741850"
FT MUTAGEN 112
FT /note="H->A: Reduces strongly citrate binding."
FT /evidence="ECO:0000269|PubMed:12741850"
FT MUTAGEN 141
FT /note="R->A: Increases citrate binding."
FT /evidence="ECO:0000269|PubMed:12741850"
FT MUTAGEN 150
FT /note="R->A: Reduces citrate binding."
FT /evidence="ECO:0000269|PubMed:12741850"
FT MUTAGEN 152
FT /note="K->A: Reduces strongly citrate binding."
FT /evidence="ECO:0000269|PubMed:12741850"
FT MUTAGEN 350
FT /note="H->L: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:10447894"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2V9A"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:1P0Z"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1P0Z"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:1P0Z"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1P0Z"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1P0Z"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1P0Z"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2J80"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:1P0Z"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1P0Z"
FT STRAND 146..156
FT /evidence="ECO:0007829|PDB:1P0Z"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:1P0Z"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1P0Z"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6LNP"
SQ SEQUENCE 547 AA; 61780 MW; 84D261862F9DE8C7 CRC64;
MSIYPMYTRK ITHWFARRSF QNRIFLLILF TSTIVMLAMS WYLTDITEER LHYQVGQRAL
IQAMQISAMP ELVEAVQKRD LARIKALIDP MRSFSDATYI TVGDASGQRL YHVNPDEIGK
SMEGGDSDEA LINAKSYVSV RKGSLGSSLR GKSPIQDATG KVIGIVSVGY TIEQLENWLS
LQISSLLIPM AIMLLLLLFC ARRFSLHIKK QMLNMEPQQL SQLLIQQSVL FESVFEGLIA
IDSDYKITAI NQTARRLLNL SQPEPTLIGK RISSVISQEV FFYDAPQTNK KDEIVTFNQI
KVIASRMAVI LNNEPQGWVI SFRSKDDINT LSLQLSQVQQ YADNLRAVQH EHRNLISTIA
GLLFLKRYNQ ALELIQQQSE SHQKVIDFIA RNFQDNHLAG LLIGKYYRAK ELGLELIFDP
ACFVDRLPTA LSHNEWISIV GNLLDNAYNA SLRQPQGSKQ IECLINSDGQ EVIIEIADQG
CGIDEALRDR IFERGVTSSA SKDHGIGLWL VRSYVEQAGG SIVVENNIPF GTIFTLYIPL
TRDEHHG
