CARS_PSEAE
ID CARS_PSEAE Reviewed; 445 AA.
AC Q9I0I2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Sensor protein kinase CarS {ECO:0000303|PubMed:26755627};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:Q8Z7H3};
DE Flags: Precursor;
GN Name=carS; OrderedLocusNames=PA2656;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=26755627; DOI=10.1128/jb.00963-15;
RA Guragain M., King M.M., Williamson K.S., Perez-Osorio A.C., Akiyama T.,
RA Khanam S., Patrauchan M.A., Franklin M.J.;
RT "The Pseudomonas aeruginosa PAO1 Two-Component Regulator CarSR Regulates
RT Calcium Homeostasis and Calcium-Induced Virulence Factor Production through
RT Its Regulatory Targets CarO and CarP.";
RL J. Bacteriol. 198:951-963(2016).
CC -!- FUNCTION: Member of the two-component regulatory system CarS/CarR that
CC regulates the expression of multiple genes involved in calcium
CC signaling and homeostasis including CarO and CarP (PubMed:26755627).
CC May function as a membrane-associated protein kinase that
CC phosphorylates CarR in response to environmental signals leading to
CC activation of specific gene promoters (Probable).
CC {ECO:0000269|PubMed:26755627, ECO:0000305|PubMed:26755627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:Q8Z7H3};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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; AE004091; AAG06044.1; -; Genomic_DNA.
DR PIR; C83314; C83314.
DR RefSeq; NP_251346.1; NC_002516.2.
DR RefSeq; WP_003090493.1; NZ_QZGE01000008.1.
DR AlphaFoldDB; Q9I0I2; -.
DR SMR; Q9I0I2; -.
DR STRING; 287.DR97_5305; -.
DR PaxDb; Q9I0I2; -.
DR PRIDE; Q9I0I2; -.
DR EnsemblBacteria; AAG06044; AAG06044; PA2656.
DR GeneID; 882365; -.
DR KEGG; pae:PA2656; -.
DR PATRIC; fig|208964.12.peg.2779; -.
DR PseudoCAP; PA2656; -.
DR HOGENOM; CLU_000445_42_3_6; -.
DR InParanoid; Q9I0I2; -.
DR OMA; NACKWAD; -.
DR PhylomeDB; Q9I0I2; -.
DR BioCyc; PAER208964:G1FZ6-2696-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..445
FT /note="Sensor protein kinase CarS"
FT /evidence="ECO:0000255"
FT /id="PRO_0000449419"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 177..228
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 236..438
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 239
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 445 AA; 49831 MW; 586B0F34061EE4EE CRC64;
MRSIQRRLSV GLFAVLLVVG LVLAQTGLWL FDQGLRRYFA GNLREEAENL LVAMVRGPNG
MQLDEQRLNP AFQRPYSGRY FVIELEKDTW RSRSLWDSEL EVPHKKGLVQ GLVDGPEEQR
LLVFRGHYKR MGQKLRIVVA QDYTPILESF ARVQWMGLGA GALALLLVLL LQRLTVRRSL
RPLEEVRLQI AQLQQGQRSQ LDNQAPEELE PLVEQINHLL AHTEETLKRS RNALGNLGHA
LKTPLAVLVS LAEREEMARQ PELQQVLREQ LEQIQQRLGR ELGKARLVGE ALPGAHFDCA
EELPSLCDTL RLIHGPHLQV SWSAPPGLRL PWDREDLLEM LGNLLDNACK WADSEVRLTV
AQGEGMVRLK VDDDGPGILP DQRQAVLERG TRLDEQVSGH GLGLGIARDI AEACGGRLSL
EDSPLGGLRV SVELPLQKSG RAARA
