ID A0A0C2Q9Q7_9CYAN Unreviewed; 1551 AA.
AC A0A0C2Q9Q7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SD81_21705 {ECO:0000313|EMBL:KIJ75085.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ75085.1};
RN [1] {ECO:0000313|EMBL:KIJ75085.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ75085.1};
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:KIJ75085.1}.
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DR EMBL; JXCB01000009; KIJ75085.1; -; Genomic_DNA.
DR OrthoDB; 5555607at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 4.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR CDD; cd21631; RHH_CopG_NikR-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 5.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; 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; 4.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 5.
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; SSF55781; GAF domain-like; 2.
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; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KIJ75085.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 117..159
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 200..252
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 253..309
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 785..837
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 852..907
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1172..1390
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1412..1538
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 72..106
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 828..855
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1461
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1551 AA; 173970 MW; 5816BB6E470495C3 CRC64;
MKRDASGKFV SNWDSQKKQR VSISLTSTAW QLLDEEAHKR GISRSEVIEH VARSFGNEAH
LDSHEIGANA QNALLQERII EQQQAIAALQ RQKQELETLL ENAPTQHEQL LHELETERTR
FEAVLRQMPA GVMIADAEGG KLVLTNEQAK QIVGYGYEQS LDLEEYAAII PFEALRSDGQ
IYTADEYPLA RSLQTGEVVS NEEIELHRED GSRIFINVNS APILDNRGQI VAAVAVFQDV
TACKLVEQAL RESESRLRGL FDANLIGIII GDFQGNILEV NDAWLAVLGY TRQEVLSGAV
NFLEITPPEF RHLDQQAMAQ MKQVGYHTPF EKEYIRKDGT RVPVLIGTAY LKGAADDLGI
GFLVDLTQRK QIEAEREMLR IRSDRHLKRE QAARRLAETE RKRLYDILMQ FPAMVAIVTG
PNLVYEFANP TYLRVAGRTP DIIGNPIRDV FPELEGQIYF DVLEEVYRTG ETFIRDESPA
YWDRNGDGVL EEAFFNCVFA AWRDAEGTIQ GVLIYNIEVT EQVRARQQIE QLLANLQHKE
RQQQFLIEVN DAIRAIQDPK EIMWQVVRAT GQHFQVTRCT YGEIDCTQEY VIVERDFCNG
VISVVGRHHM DSFGPAIIAE LKQGKTIVVD DVDVDPRTAG VGVAAFNAIQ TKSLVCVPLV
KEGRFVALFV LHHVSPRRWA AEDVALMEQI AEQTWLAVER SRAEEELRES EAHLQLALKV
GRMGTWDWDM QTDTLLWSEG HFTVLGLQPN ECEPSHEVWA SRIHPDDLTQ AEAKFQQAML
GKNEYDHEYR LRWSDGSIHW VEVRGQFTYD SGGNPKHSIG VVIDITERKQ VEQEREQLLK
RERIARAQVE AAQRQLTTIF ETSPVGIALL DTEQRFIAIN EALAQINGLT REQHLGYSIA
ELFGQSDPQI VEVFHQIYTT GNPFISPNFA VNVPGRSDRT PGYYNVYYLP TMNSNHQVED
VLVYVVDVTE QVRLERAQHF LSEASAVLAS SLDYQTTLER VAQLAVPALA DWCTVHMVEE
DGSIEQIAVA HTDPAKQQWA HQIRHQYPLN PDEPRGAALT LRTGQSDLLA DIPDELLIQA
ARDPEHLEIL RQVGFKSVMT VPLRTQARIL GVISFVSAES GLQYDSIDLQ LAEELAHRAS
LAIDNAQLYR VAQRDRAKAE AANRVKDEFL AVLSHELRSP LNPILGWTKI LRSKRLDPTK
VDQALETIER NAKLQAQLIE DLLDVSRILQ GKMTLNVAIV NLAATIEAAL ETVRLAAEAK
NIQIQTTLNP ISGTVCGDGN RLQQVVWNLL SNAVKFTPSR GRVEVRLEQV GMYAQIQVKD
TGIGISPEFL PYVFEYFRQE DGTTTRKFGG LGLGLAIVRH FTELHGGTVE ADSPGQNLGA
TFTVRLPLNL VQEELSADHS QKESVTDLTG IQILVVDDDA DMRKLAEFIL TQSGAQVTTA
ASGAQALTLL NQSVPDLLLC DIGMPEMDGY SVIRQIRKWS ARQGGTIKAL SEALPKAIAL
TAYAGEINQQ QALAAGFQMH ISKPVEPEKL VQAIVQLLHP ISQANHRQHT D
//
