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Database: UniProt
Entry: Q2RNY8_RHORT
LinkDB: Q2RNY8_RHORT
Original site: Q2RNY8_RHORT 
ID   Q2RNY8_RHORT            Unreviewed;       515 AA.
AC   Q2RNY8;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 122.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Rru_A3363 {ECO:0000313|EMBL:ABC24157.1};
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC24157.1, ECO:0000313|Proteomes:UP000001929};
RN   [1] {ECO:0000313|EMBL:ABC24157.1, ECO:0000313|Proteomes:UP000001929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC   {ECO:0000313|Proteomes:UP000001929};
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC24157.1; -; Genomic_DNA.
DR   RefSeq; WP_011391110.1; NC_007643.1.
DR   RefSeq; YP_428444.1; NC_007643.1.
DR   AlphaFoldDB; Q2RNY8; -.
DR   STRING; 269796.Rru_A3363; -.
DR   EnsemblBacteria; ABC24157; ABC24157; Rru_A3363.
DR   KEGG; rru:Rru_A3363; -.
DR   PATRIC; fig|269796.9.peg.3477; -.
DR   eggNOG; COG4251; Bacteria.
DR   HOGENOM; CLU_000445_114_71_5; -.
DR   OMA; DNTITHA; -.
DR   PhylomeDB; Q2RNY8; -.
DR   Proteomes; UP000001929; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABC24157.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001929};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABC24157.1}.
FT   DOMAIN          9..53
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          76..129
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          130..200
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          203..256
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          274..491
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          491..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  57121 MW;  2D958CD8505380E3 CRC64;
     MSGEPVGLAL QRLYDLTRLV SDWIWETDSA GLLTYASDRV FEILGYPARA LIGHPFAELA
     ASGDPPFFKS DPRPFREQRF EARHSDGSPR VLLISAVPLF DAQSGDRQGW RGAAKDITQS
     ERADAEMDRQ RRFQQTLLDA IPLPVFLKDR EDRYQGCNLA FETASGRSRA EILGQRMEQV
     LRSENYDRHR AEEALVLREG RTRVWEAMEH DVSGRHKLIS ITASPYREPG DPTVRGLIGV
     VSDITRRQRA EDALRASVVE LTASNRELQH FAEIAAHDLQ EPVRAVVSHC QLLERHLGDA
     LDGPARDHMI FAITGARRMR DLIQDLLIYA RAGRDGQFHE VVDTADLARE VVSALADEIA
     ASGATIRIDP LPSVLGRRRD LFDVMVNLFD NALKFRRPDV VPEVTLKAAE TLDASGLWCF
     TLSDNGIGLD PVHGAQIFAL FRRLHGADRY PGTGVGLAIC RRIVEQHGGT IFVESAPGVG
     TRFHFTLPAA PSEEPDRLVG RGTRSAPRPV IDGGG
//
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