ID A0A0P8C255_9CYAN Unreviewed; 1008 AA.
AC A0A0P8C255;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HLUCCA11_10410 {ECO:0000313|EMBL:KPQ35365.1};
OS Phormidesmis priestleyi Ana.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Phormidesmis.
OX NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ35365.1, ECO:0000313|Proteomes:UP000050465};
RN [1] {ECO:0000313|EMBL:KPQ35365.1, ECO:0000313|Proteomes:UP000050465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ana {ECO:0000313|EMBL:KPQ35365.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPQ35365.1}.
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DR EMBL; LJZR01000012; KPQ35365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8C255; -.
DR STRING; 1666911.HLUCCA11_10410; -.
DR PATRIC; fig|1666911.3.peg.4228; -.
DR Proteomes; UP000050465; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; 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 InterPro; IPR007890; CHASE2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01080; CHASE2; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:KPQ35365.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 383..658
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 685..805
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 888..1004
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 831..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 735
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 937
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1008 AA; 111055 MW; C7AD9BB417A6FA6A CRC64;
MLSKIRRFSG LNRLLRKRLG CIIPSLVASL IVAALIQLNV WVPLERAVNN QMMVWRGTRD
WDSRIVMISI DNKTLDAYGQ FPISREYYAD LLLKLIQEES SVVAFNILFA DGSTSSRAPD
SSAINAKLAN AIATSGNVII GQAWDEEGLA LLPVPVLADT VIAVGHLQFE SDPDGIVRRV
PITWDNVPTL GAATVQAYSL QKELISIPSN LQTLHINWPN SATQLTTLSL VDVLGGNIPA
KYLKDKIIIV SYGATAGQVQ LRTPFDRLRP VPAGYLHAAV IDTLLKQNWL RPISSNVIIL
IVLIGSPLFG ALLYRRTTFV QLLIGIGAFV AWLVICMVAL YFDYLLPVVP PLATLGLTGA
TVITLSHLQS NALLQVRSAF LNTISHEIRT PLNAIVNLSE MLQETQLDNR QREFAETLNT
SSQTLLALIN DVLDFSKIES GRLTIEAYPV RLNDTLERCL EMLSPKAAEK DLELVYSIAP
GTPTVVMSDP VRLQQILLNL LSNAIKFTAT GEISVQVQAI VLASNPSLFS LKQRQVIQWM
RSLQSNARAN TRANARANAR AASATKLQPP PSADYRIGNL YEIRFAVHDT GIGIPPERMG
QLFKPFSQVS TATTRKYGGT GLGLSISKRL SDRMGGDLWV RSYPGQGSTF YFTVQAYEAL
PHLSLGATSK TGHQPTYLTG LNGARILLID RNITRRSQLN WELQLLGIRL AQATSLSEAL
AFVQNGPTFD GLILDEAILY SPEECATTIQ TLRQTARNDY LPVILLSKLR AQAHHPPIGS
LLSQTTIIWK PVKQAALYQA LRSIEAISLS LSGSNNNSNR APAIEPALKR TLDGPLEPDS
KQSPEPSSER SPEHSPECSP ECSPECFPES GHLALEPSLE PSHPVSLDIL IAEDNPVNQR
VALRLLELLG YQADIAASGL EVLTALNRQR YDVILMDMRM PDLDGIETTR QIRQMPQYKD
IWIIAMTANA MERDRQRCFA VGMDDYLSKP INRNALNQAL KRCPADRP
//
