ID A5V1R1_ROSS1 Unreviewed; 718 AA.
AC A5V1R1;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=RoseRS_4482 {ECO:0000313|EMBL:ABQ92814.1};
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ92814.1, ECO:0000313|Proteomes:UP000006554};
RN [1] {ECO:0000313|Proteomes:UP000006554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000686; ABQ92814.1; -; Genomic_DNA.
DR RefSeq; WP_011959151.1; NC_009523.1.
DR AlphaFoldDB; A5V1R1; -.
DR STRING; 357808.RoseRS_4482; -.
DR KEGG; rrs:RoseRS_4482; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_381229_0_0_0; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000006554; Chromosome.
DR GO; GO:0016020; C: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; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF33; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABQ92814.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ABQ92814.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 497..715
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 187..214
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 718 AA; 78217 MW; C08C275408638616 CRC64;
MIAGDTLTRQ LPYWLIERRA YLGQMLAPAP ALALAVWLSA AAPPEALWMA LIAYALVHLW
LFWVAYHHPV GIDPRAPGAG WVAIGVDALL GAIVVSGATD LSFFLPVYTL IAWRALSGYG
RNQAALAPLF AIGPLFLFQF LLSRAGSASL TAGEQWSAAG VLAGSLGCGI VAIMTGARQQ
RSIMRLRSEL QRERNTREAR VEELEHLANE LRLRMRERHA LEEGLRAVTS TLSLDDVLEQ
ILDSTVQTFG AERTHAVVLT LATDGTLTNR VYARDGQMRP QWVEPLIRRV MHDQAPAVVA
DAALDAELGA ISRSGLRSIV CVPLFVGDGP PRGALTVVSA TFAAFSSSDA RHLAAFAAQA
GIAIGNAELH SRLRRQQQLL QAVLRDINDG LVVLDNEYNV VLANPIGQAL LNDTSAPQPW
LERMRELASR LSDDGRPVAS PEWVFGSPDA EEGQIVYQAV ASRVHTDDDL PDLTAIVLHD
ITDHKAEERA RMDFISMVSH ELRNPLHTLN GFVKLVLQER AGPLTSLQQD FLKMADEQIE
QLSSRVAELL EYNRFKAGRL ALQPDVGDLA LLIAGTVNRL KLQAEQQQLA LVSHVTHLPL
CRFDGQRIGQ VLTNLIENAI KATPAGGTIS VSADVHDQEV RVRVSDTGVG IPASELGKIF
QRFYQVAKHR RTHGNNLGLG LAICQQIVEG HGGRIWVESE EGVGTTFTFT LPLADGQA
//
