ID K9RHZ1_9CYAN Unreviewed; 760 AA.
AC K9RHZ1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Riv7116_4288 {ECO:0000313|EMBL:AFY56717.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY56717.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY56717.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY56717.1,
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; AFY56717.1; -; Genomic_DNA.
DR RefSeq; WP_015120279.1; NC_019678.1.
DR AlphaFoldDB; K9RHZ1; -.
DR STRING; 373994.Riv7116_4288; -.
DR KEGG; riv:Riv7116_4288; -.
DR PATRIC; fig|373994.3.peg.4574; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_72_3; -.
DR OrthoDB; 9789238at2; -.
DR Proteomes; UP000010380; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 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 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; 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; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010380}.
FT DOMAIN 6..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 262..336
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 341..394
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 395..467
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 544..760
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 760 AA; 87351 MW; 053874FC2DF142DD CRC64;
MQNHYTVLII DDCLEDRNTY CRYLQKDDEC NYQFLEQEYG KDGLEACKQV QPDIILLDYM
LPDINGLEFI QELQSCCKDT SPPIIMLTGE GSEKIAVQAM KYGVEDYLVK ANTTAKILRL
TVRNVIEKKN LQQKLEVSKR RFFTSVENMF DCFGIYVCIR DDNGRITGFH REYLNAAAWE
NELIGLEEHG SQEEEELFKE YCQVIETGKS FLKEVLCFSN HNNQQVLSKA YDVSISKLEN
GFVATWRDIT KRKISEQALQ ESQHLIQRIA DTTPDILYLF DLEEQRNIYI NRQVQQRLGY
SPLLIKKMGA DLFKNLVHPD DFQRLKNHLK KFASIKDGEI LPFEYRIRDI QNQWHWFSSR
DTVFTRSSDG KPQQLLGVVR EITAQKQSEE ALRESEARFR YIYESNMLGI MFWKTNGKVI
DANARFLEII GYSREDLQAG LIRWDEFTPP EWKEVDREAI EQIKNNRVCH PFEKEYIRKD
GSRVPIVLGA CLLENSINTG VSFVIDITER KRIEKERAQL LISEREAREQ AEAANLAKDD
FVAMVSHDLR SPLNAILGWS QILRSSSKDE AIKNRGAEII ERNAKAQDAL IQDLLDISRI
IRGRLQLQMI PVKLESILNN AIDSAYPVAI AKNIHLESEV DSNINNMLGD AKRLQQVVDN
LLSNAVKFTP ESGHIKVNLR KIENNAQIKV IDTGSGISKE LLPLIFERFH QGSNIETKQQ
GLGLGLAIAR HLVELHNGKI TAESRGEGKG TTFTVILPLQ
//
