ID K9RBB0_9CYAN Unreviewed; 1065 AA.
AC K9RBB0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Riv7116_2743 {ECO:0000313|EMBL:AFY55245.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY55245.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY55245.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY55245.1,
RC ECO:0000313|Proteomes:UP000010380};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL Submitted (AUG-2012) 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; CP003549; AFY55245.1; -; Genomic_DNA.
DR AlphaFoldDB; K9RBB0; -.
DR STRING; 373994.Riv7116_2743; -.
DR KEGG; riv:Riv7116_2743; -.
DR PATRIC; fig|373994.3.peg.2908; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_114_18_3; -.
DR OrthoDB; 9758522at2; -.
DR Proteomes; UP000010380; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 4.
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; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 5.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010380};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 138..212
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 215..268
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 269..343
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 345..397
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 398..470
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 474..526
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 694..765
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 769..821
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 853..1064
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1065 AA; 122502 MW; 6AA6C3BB03F32EFF CRC64;
MLLISANFLA TASLMPHGNC YLWKPGLVGL HMVSDAVIAL SYFSIPITLL YILRQRADVP
FNGIFWLFAA FIIFCGTGHL IDIWTLWHPD YWISGYVRAM TAVVSFITAI VLTYLVPQIL
TLPTPEKLQA EIEEKKQKEQ FLRSIYEGVT EAIFVVDTTK EGEFIYESIN PVTEKLMGMT
SKQVEGKTME QVLPHNLALL IRERYNQCLS TGRSITYEEC LRFDDDSEYS WWLTNLKPIY
NQNSQIYRIV GTSVDITERK QAEARLRESE RRFRAIFDSM YQFIGLLKPD GTLLEANQTA
LDFGGITKED VVNCPFWENY WWTISPETQQ QLQQAIKRAA NGEFVRYEVD VLGAGNKVTT
IDFSLKPVFN DLGKVELLIP EGRDITEKKQ IIEALQKSEE RWNLALLGTG DGIFDWDLST
NEAFFSTQYK EMLGYADSEV ENSYQGWRDL VHPEDIDLAE ATWKAYINHE IPQYRAEFRL
RCQDGSYKWI LARGMAQWNQ DGEAIRMVGF HQDISERKAA QAEIVRLNQQ LEARVKRRTA
QLEESNKYKD ELIESQEIAK AEIQIYEDIV ENIQIGLCIW QMDDINDITS FRLATINPVA
SQMLGVNIED DIDKPIKECF PNLFDDEHIA IVEAYAEVVK SKQVKDFGEF AYGDDRVPNS
WFEVTAFPLP DNLVGVAFNN VGERKRMETA LAENERLYRN VVNSVKEVVF QIAKTGIWTF
LSAAWADITG FAVEDNLLKT FTDFMYAEED KLNSRELFES VISGKQEHFQ YEFRILTKDE
NFRWLEIYAQ IEHNSNGETL GVYGTLNDVT ERKQVEAVLQ ARADELAQIN LILLQTTGEL
EKRNQELDQF AYVTSHDLKA PLRAIANLSE WIEEDLQEAL TPDTQKQMNL LRGRVYRMEA
LINGLLQYSR VGRMKTEPEK VAVAQLLEEI IDSIAPPQEF TIEIIGEMPT FRTAKIPLQQ
IFTNLIGNAV KHHNRSDGRI AISVLEQDKF YEFAIADDGK GIAEKYHDKI FVIFQTLESR
DKRENTGIGL AIVKRIIEEF GGKITLDSQL GKGTTFRFTW LKKRM
//
