ID A0A3N6RFW8_9CYAN Unreviewed; 958 AA.
AC A0A3N6RFW8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 08-OCT-2025, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D5R40_14955 {ECO:0000313|EMBL:RQH42203.1};
OS Okeania hirsuta.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Okeania.
OX NCBI_TaxID=1458930 {ECO:0000313|EMBL:RQH42203.1, ECO:0000313|Proteomes:UP000269154};
RN [1] {ECO:0000313|EMBL:RQH42203.1, ECO:0000313|Proteomes:UP000269154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAB10Feb10-1 {ECO:0000313|EMBL:RQH42203.1,
RC ECO:0000313|Proteomes:UP000269154};
RX PubMed=30444349;
RA Moss N.A., Leao T., Rankin M., McCullough T.M., Qu P., Korobeynikov A.,
RA Smith J.L., Gerwick L., Gerwick W.H.;
RT "Ketoreductase domain dysfunction expands chemodiversity: malyngamide
RT biosynthesis in the cyanobacterium Okeania hirsuta.";
RL ACS Chem. Biol. 0:0-0(2018).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQH42203.1}.
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DR EMBL; RCBY01000077; RQH42203.1; -; Genomic_DNA.
DR RefSeq; WP_124154822.1; NZ_CAWOLW010000692.1.
DR AlphaFoldDB; A0A3N6RFW8; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000269154; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR051315; Bact_Chemotaxis_CheA.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR003594; HATPase_dom.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RQH42203.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000269154};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 388..658
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 839..956
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 889
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 958 AA; 107831 MW; 94E6D951A1EC36A0 CRC64;
MIEIDDQAYK FFVEEATELL QTLEQGLIHI SQEHELQKLH QLMRAAHSIK GGAACIGLMG
IQTIAHDLEN SIRALYQENT VFDLELENLL LQAFDCLRSP TVKQIETGNY DQENSIIKAK
QVFEQIEKKL GHSLEEAAEF PEVSMEEGDM TKFLFTEEIP SGLHRWENLL AGKNSTDSGL
SIKDELKRQA EVFATLGTML NLPGFTSIAQ TTIKALEVNP KYIKKIGTLA LADFWAGQKA
VLAGDRTQGG NLNPTLVKLT KPLKSRKVET TAKRKQVNQP TQAVKAVVPQ KSEVAVETEN
VKTSNSATSS VNISQKQVSA PGVANQKKQI QQKQITSTSS SSLGVRIDIN RLEMLNNLLG
ELATQDNSFI LQNQQSQASI GTLEKGWQKF HQLMMKLQDM KTFSEQLNKS PNSQNNQLAY
LVNILPNLLE EIAQVGEAVN DIKLLHQQSQ QVVKKRQQTL QQIQNNLTKT RMLPVESLLN
RFPRMIRDLS VQKQKQVKLE LVGMNTLIDK VVLEKLYDPI VHIVRNAFDH GIEPPEIRQS
NGKSKEGQIT IKSYYQGNYT YIEIRDDGRG IDVNKIRNLA IQKKIFSVTE AAKLSTKQLY
KLLFYPDFST TKKVSDLSGR GMGLESVYSQ IESLKGNITI QSQLGQGTKF ILRLPWTLTI
TKLLVFRMEG NFFAIPLDIL AAIIYVDPSE IKVERREKVY YWKGKKVSIA PSILLDYNYP
IVSGSIQQES VEFSWKNSYT KNSQGKVMLL LISEDSDTIA IKIEQILMEQ NLTIKPFSKI
LKAPSYLYGC TILGDGSLVP VIDGIQLLEK ILHTEQLDAK NLLKNTSKFK QSILSKLPTI
LVIDDSLTTR QAISSTLQKA GYDIVQAKDG WQGLVKLQQN TQIQAVICDV EMPQMNGFEF
LSRCRKQYPI AQMPVLMLTS RSSQPYRTLA KQLGANDYLS KPYLDQELIN SLQSCLQV
//
