ID L8N0R4_9CYAN Unreviewed; 1355 AA.
AC L8N0R4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-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=Pse7429DRAFT_2498 {ECO:0000313|EMBL:ELS32320.1};
OS Pseudanabaena biceps PCC 7429.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS32320.1, ECO:0000313|Proteomes:UP000011201};
RN [1] {ECO:0000313|EMBL:ELS32320.1, ECO:0000313|Proteomes:UP000011201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS32320.1,
RC ECO:0000313|Proteomes:UP000011201};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ELS32320.1}.
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DR EMBL; ALWB01000101; ELS32320.1; -; Genomic_DNA.
DR RefSeq; WP_009627566.1; NZ_ALWB01000101.1.
DR PATRIC; fig|927668.3.peg.2902; -.
DR OrthoDB; 502671at2; -.
DR Proteomes; UP000011201; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd12913; PDC1_MCP_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR029151; Sensor-like_sf.
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; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELS32320.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 369..421
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 444..519
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 522..573
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 880..1117
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1143..1259
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 413..447
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 846..873
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1192
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1355 AA; 153623 MW; 701A0B66F641A673 CRC64;
MSDRLAFPNP QKPRKLTLKF ILIGQFAILI IGISGLMAWL SWHSEQETID NLVGQLQNEI
SDRIEQKLTS YLEVPHLINR INADAIGQGI LKTQDRASEK YLWQQINNFP MVSWIYYGEE
STGNFVGITR IDNKLQTAIN INGSKGLQRY RYNLNRQGER LSLAGNPEAY DPRQRPWYRA
ALRDRQSTWS PIYQDFNRPE QVITASLAVY NAEGKRIGVL GTDLSLGSIS QFLNSLQIGK
TGQAFIVEPS GLLVASSVRE NLYDLTSQRV PLKNVKQPMI RMAANYLEQQ AGGLDHLNTA
QNLKFQSEGK NIFLKVLPYR DNRGLNWTIV VTVPESDFTE QLDLKRQRTI LLIGLCLAGA
IALGIFTTQY INRPLRRLTL ASQAVTNGEL NREVPSAAIE EMDLLSQAFN QMAFRLKLSF
DELERANENL ESRIQERMTD LQASEEKFRS LVSNFSGIAY RCNGDRDWTM VFIGGDVEGL
TGYQPEDFVA DRVRSWTSII YPEDRDYIKR GINESLACGQ PYSLEYRIIN AQGNIRWLCE
KGQGIFADDR LLWLDGAIFD ISDRKQVEAE LLERVHLSIL MAEIGSASTQ LHTLAEVLQS
FVESLWRHMN VAFAQIWTLN AFGNSLDIDV SAGNYNHTDR ERLRHLIPQA KIWSITQGNF
QPLLTNQILA DISEVDRQWL QEENIISLVG YPLIVKGKVI GVILMLSQSH LDTDIQTIDL
ISNAIAIGID HKQSEEKLRI TNAEMQALFA AMDDVILVRD RLGRILKTPE TRKGNWRESR
EIIGKLPSEI FPQEQVELFT NCIEQVLETQ QTLNVEYLSS NDQAIDRSIW WNASISPIDR
ETVVWVARDI TDRKQVEEQL KQAKQTAESA SQAKGHFLAS MSHELRTPLN AILGFTQLML
RDLSLTDSHR SYLKVIHDSG EHLLELINDV LDMSKIESGR ITFNSTCFDL YRMLDMLEQM
FRLKAIDRKV KLIFKRSPKL PQWIVTDEGK LRQILINLLS NAIKFTKQGS ITLSAEALHP
EETNGLGGES PLNPQKEASS GTIIFKVEDT GEGIPPHQLE RIFEAFEQTD IGRRASEGTG
LGLPISLKFA QFMGGQITVS SILGEGSTFQ VEIPISISAE SVPLHQPNDL YVTALAPDQP
EYRLLVVEDR WESRHLLVKI LEAVGFQVRE AQNGAEALAL WEEWQPHLIW MDMRMPIMDG
YEATRQIKSH LRGQATVIIA LTASALEEEK AIILSAGCDD FVRKPFQENL IFEKLTEYLG
VTYLYEHESD RHIKGKNNLD LEALKANFTA NLSQMSDLWI AQLNQAAMLA DNDLINELVA
EIPEDNTVLI HSLIALVDNF CYNQIMGLTK QALRK
//
