ID C4LLE9_CORK4 Unreviewed; 375 AA.
AC C4LLE9;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=tcsS4 {ECO:0000313|EMBL:ACR18654.1};
GN OrderedLocusNames=ckrop_1941 {ECO:0000313|EMBL:ACR18654.1};
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR18654.1, ECO:0000313|Proteomes:UP000001473};
RN [1] {ECO:0000313|EMBL:ACR18654.1, ECO:0000313|Proteomes:UP000001473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC {ECO:0000313|Proteomes:UP000001473};
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR18654.1; -; Genomic_DNA.
DR RefSeq; WP_012732541.1; NC_012704.1.
DR AlphaFoldDB; C4LLE9; -.
DR STRING; 645127.ckrop_1941; -.
DR KEGG; ckp:ckrop_1941; -.
DR eggNOG; COG2770; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_3_11; -.
DR OrthoDB; 9757990at2; -.
DR Proteomes; UP000001473; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACR18654.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001473};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..142
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 150..367
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 375 AA; 40185 MW; 2B32979EB47BE216 CRC64;
MNHGPGLTFR FLAAQVLVVV ISLLVAAAVA TMVGPTLFHD HMLMTGREDP SLELFHAEQA
YRGANLITLA VALPTALISA LLASLCLSRR LRTPLQDLTH AATSLTAGNS RIRVPAGKAG
PEVTTLAHAF NTMADRLEHT EQVRRQMLSD LAHEMGTPLS VLTVYLDGLQ DGVVDWNNAT
HTIMADQLTR LTRLMEDIDD VSRAQERRID LDLAEEGLGD LLHTAAAAAG EAYADKGVDL
QVETITDTAR VLVDRQRFGQ VMSNLLSNAL RHTPAGGQVR ISVHRQGAST ALIHVVDDGD
GIPPDQLRYI FERFYRGDAA RSRDDGGAGI GLTISKALIE AHGGTLTATS PGPGRGAVFA
LRLPLSPPDS EEAAR
//
