ID Q4JSW5_CORJK Unreviewed; 432 AA.
AC Q4JSW5;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Sensor-like histidine kinase SenX3 {ECO:0000256|ARBA:ARBA00039401};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=tcsS8 {ECO:0000313|EMBL:CAI38092.1};
GN OrderedLocusNames=jk1911 {ECO:0000313|EMBL:CAI38092.1};
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI38092.1, ECO:0000313|Proteomes:UP000000545};
RN [1] {ECO:0000313|EMBL:CAI38092.1, ECO:0000313|Proteomes:UP000000545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411 {ECO:0000313|EMBL:CAI38092.1,
RC ECO:0000313|Proteomes:UP000000545};
RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CR931997; CAI38092.1; -; Genomic_DNA.
DR RefSeq; WP_011274216.1; NC_007164.1.
DR AlphaFoldDB; Q4JSW5; -.
DR STRING; 306537.jk1911; -.
DR GeneID; 3433248; -.
DR KEGG; cjk:jk1911; -.
DR PATRIC; fig|306537.10.peg.1939; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_11; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000000545; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:CAI38092.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW Transferase {ECO:0000313|EMBL:CAI38092.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..386
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 393..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 47237 MW; 7312A7555C3CB58C CRC64;
MGLLTSEVAL GLLFGLIVGV CLGAFGMWAY RKRVKAQRNT HTQRELEGNR VSTVAQVLHF
AIQSSPDAVA VVDRKRNVVL SNPRAHELGL VHERNLNAEA WKMVERVFAD QEPRELNFLP
PPRRSNRPVI AVAGQVQLLS LADDRFAVVY ATDDSESVRM ESARRDFVAN VSHELKTPVG
AISLLVETLM SVRDDEEAVE YFGSKLIVEV RRMNQMITEL ISLSKLQGAE SLPDLEVLSI
DKVIEDAIDR CRLAAEARNI DLVKDGRSGA MVKGDKGLLV TSVANLLTNA INYSPEGSPV
SISREADGDN VIIRVTDRGI GISQDDQKRV FERFFRVDKA RSRDTGGTGL GLAIVKHVMA
NHGGSVSLWS RLGTGSTFTL ELPRFQEGKA KELPSGEIPV IPDARRLDVA QGTGGTTGPL
GTEGRDPDIE DK
//