ID A5UPW4_ROSS1 Unreviewed; 844 AA.
AC A5UPW4;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=RoseRS_0231 {ECO:0000313|EMBL:ABQ88667.1};
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ88667.1, 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; ABQ88667.1; -; Genomic_DNA.
DR RefSeq; WP_011955026.1; NC_009523.1.
DR AlphaFoldDB; A5UPW4; -.
DR STRING; 357808.RoseRS_0231; -.
DR KEGG; rrs:RoseRS_0231; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_0; -.
DR OrthoDB; 9784397at2; -.
DR Proteomes; UP000006554; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13185; GAF_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABQ88667.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABQ88667.1}.
FT DOMAIN 489..703
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 724..840
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 773
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 844 AA; 93499 MW; 5006E67421DA78BC CRC64;
MGYSPAHDQP ESADLLFEVI DHIPAGILVV SLPDFRILAI NARACARLGI RISATLTGRL
CRDVIPRFSD DRLDDLWLSM AGLRHDDTVP ATQIGGVVSR RWNAYPVRDQ HGHAVRLLLV
WLEAGETPEH QFASSAQHIT QALISTLDRD QLLDLILEHL HSIVSYDSAA IILRDDDGYY
IAASRGLPDR TAPTYQRLPK DNALLNRIET VGEPVIVRRL PEDAIEAMCS LSNAPGEWLS
VPLRAQGDVV GMLTLFSRLP NRYTRADAAR AQAFATYAAL AVRNAELYRR AREQSARLAL
VNKIARTITA THDLRAIFDH LIEHLHGVVP LDSAELALFD RTAQHLQPVA HYPASDNTET
LCVHYHDQDT IFLRRLIEQR QPVLLPLDDT GNPPLTQRLV AAGIRSCLIV PIVDGENLSG
MLLLASRQSN AFPAIEIRTF ADLAQHLAVA IQNAQLHQAR EQAIANLRIA QQRLIQSERL
TAVGELVAGV AHELNNPLTA VLGFAGILQE VAPAEYQHDL TMIVESATRA RRIVQNLLTF
ARQREAHLEE VDLNLAARQV LSLLAYQMRT HNITVEERLQ PQLPLTVADA TAIKQVMLNL
LNNAQQALAS WSGRRTIVVT TRLELRENRQ WLVLEIADTG PGIAPEHLPR IFEPFFTTKP
VGEGTGLGLS ICYGIVRQYH GNIRVQSAPG KGACFTVELP VQSFVSVPST RDTTVTVQPS
SRYHILVVDD EAAVAELIAR LLREQRCIVD VCHDGAQALD LLSRVAYDLI ICDVRMPGMS
GDELFVELKQ RAPHLVRRVL FVSGDTASRS TRDFFERSGV GYIEKPFTAS ELIDAVQRSL
AAVS
//
