ID A0A0C2Q5F3_9CYAN Unreviewed; 630 AA.
AC A0A0C2Q5F3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SD81_24260 {ECO:0000313|EMBL:KIJ75488.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ75488.1};
RN [1] {ECO:0000313|EMBL:KIJ75488.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ75488.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) 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};
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:KIJ75488.1}.
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DR EMBL; JXCB01000009; KIJ75488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2Q5F3; -.
DR OrthoDB; 9788063at2; -.
DR GO; GO:0005524; F:ATP binding; 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; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-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; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KIJ75488.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KIJ75488.1}.
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 133..203
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 270..492
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 511..627
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 562
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 630 AA; 70273 MW; 0DADC01AA2B6BD05 CRC64;
MKDSIFKVLL VDDDEDDYIL TRDWFREFQV ANCELEWVNT YQAAMEAIGN NQYDIYLVDY
RLGARNGLDL LREAIAKGCS SPIILLTGKG DREIDIEAMK AGAADYLEKS QLTAPLLERS
IRYAVERKRA EQRIREHAAL LDVATDAIFV HDLKNKILFW NKAAENLYGW RATEAIGKKT
LELWKEKDSS QFQEALKSLL QNGAWEGELH QKTKFGKEII VESRWTLVQE FNKKGQSILV
VNTDITEKKE LEAQFFRAQR LESIGTLASG IAHDLNNVLA PILMTAQLLE SQLHDERSKR
LLPILISNAK RGANLVKQVL SFTRGMEGDR TLLQLKHLIR EIQQVVKETF PKSIEISTHT
APNLWTVSAD ATQLHQVLMN LCVNARDAMP DGGRLSISAE NLVVDQNYAK MYLDARVGSY
VVITVTDTGI GIPQEILDRI FEPFFTTKEL GKGTGLGLST VVGIIKSHGG FINVYSEVGK
GTQFKVYLPA QEAAENPEEQ EPELPCGNGE LILVVDDEDS IRDVTKTSLE SYNYKAITAC
DGIEAIALYA EHQDEISVVL TDMVMPSMDG VTTIRTLRKI NPAVKIIAVS GLASSEKINT
VTDMGVKAFL SKPYTAKQLL QTISTVTSGN
//
