ID A0A0J9HL90_9CYAN Unreviewed; 1061 AA.
AC A0A0J9HL90;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 08-NOV-2023, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=WN50_38815 {ECO:0000313|EMBL:KMW69994.1};
OS Limnoraphis robusta CS-951.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX NCBI_TaxID=1637645 {ECO:0000313|EMBL:KMW69994.1, ECO:0000313|Proteomes:UP000033607};
RN [1] {ECO:0000313|EMBL:KMW69994.1, ECO:0000313|Proteomes:UP000033607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-951 {ECO:0000313|EMBL:KMW69994.1,
RC ECO:0000313|Proteomes:UP000033607};
RA Willis A., Parks M., Burford M.A.;
RT "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT robusta strain CS-951.";
RL Submitted (JUN-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 -!- 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:KMW69994.1}.
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DR EMBL; LATL02000312; KMW69994.1; -; Genomic_DNA.
DR RefSeq; WP_049561273.1; NZ_LATL02000312.1.
DR AlphaFoldDB; A0A0J9HL90; -.
DR PATRIC; fig|1637645.4.peg.6175; -.
DR OrthoDB; 567946at2; -.
DR Proteomes; UP000033607; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; 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; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
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; 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; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 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; 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); 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KMW69994.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000033607};
KW 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..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 384..436
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 441..479
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 518..572
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 608..832
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 858..974
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 563..608
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 907
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1061 AA; 120304 MW; 300B9A9774C3AD80 CRC64;
MPIKPFAKVF ARLPLRVVLI VPFVLQIFGI VGLVGYLSYK NGQKAVEDLA HQLMDEVGDR
VDQNFSNYLN TLEKVTRNNA EILKMGILPS DDLELLQRYF WQQIKIFDRA NAIGIVTETK
DFLLIEAIEP GSLVLRISNQ STQGEQYNYK LNEQGNPIQL IETHRYDPHN DPPGNPWYSR
TREAGELIWI HSVSAPLGYD KPIVTLVNFQ PFYDQKGNFS GVVTAAFHLS QIGDFLAKLA
IGKTGETFII NSEGFLIATS TGELPFNQNI NINKAQSLNP QKRKKLAINS QSFLVRSATQ
ALFYHFPSLK HIDHRQQLKF KLDNKSYFLQ VSRTQQDKNL DFLTVIVVPE SDFMARIHAN
TKTTVILCII ALTVATLLGI LTARWLTKPI LKLNQAAKDI AQGKWDKITE IKRTNELGEL
ADSFNQMADQ LQTSFAELKD SEHRLIQYLE ALPVGVSVHD KTGKVYYTNQ ASRKLLNIQS
PLDAETKELS QAYQIYQAVT GKLYPTEALP VVRALTGKTV YADDLEVQYR DQILPLEVWA
TPIYNEQGNI IYTIAAFQDI TQRKQAEQLL ADYNRTLEIQ VAQRTQELAE AKEKAEVANR
AKSEFIANMS HELRTPLNAI LGFSQLMTDS NDLSSDHRED INIIKRSGEY LLTLINNILD
LCKIEAGKIT LNLKSFDFYR LLDEIEELFK FKSINKGLQL DFERADDVPQ YIQTDEIKLR
EVLINLLSNA MKFTKVGGVS VRVKSLSTPE TEPLTQTLYF EVEDTGVGIA PEELNQLFEA
FSQTQSGKQA QEGTGLGLAI SQKFVQLMGG EINVKTQVGI GSVFSFNIQV NLVNPTEVET
KISQRRIIAL EPNQPSYKLL IVDDNLINRK LLIKLLNPLW FELQEATNGK EAIKIWQDWE
PHLIFMDMRM PVMDGYEATK QIKTTIKGQA TAIIAITASV LKDDKNIILS AGCDDFVRKP
FEESIIFEML EKHLGVRYVY EETHLAEKET ISYTLDAERL KVMSADWLEE VYQASMDLDD
DCILTLIAQI PENHATLAAA LTDCVQNFRF DKIIDIIEPI R
//
