ID A0A0P7ZZ54_9CYAN Unreviewed; 1024 AA.
AC A0A0P7ZZ54;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HLUCCO16_00425 {ECO:0000313|EMBL:KPQ40828.1};
OS Phormidium sp. OSCR.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=1666905 {ECO:0000313|EMBL:KPQ40828.1, ECO:0000313|Proteomes:UP000050461};
RN [1] {ECO:0000313|EMBL:KPQ40828.1, ECO:0000313|Proteomes:UP000050461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSCR {ECO:0000313|EMBL:KPQ40828.1};
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:KPQ40828.1}.
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DR EMBL; LJZT01000001; KPQ40828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ZZ54; -.
DR STRING; 1666905.HLUCCO16_00425; -.
DR Proteomes; UP000050461; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
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; PF08448; PAS_4; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KPQ40828.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:KPQ40828.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 471..542
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 541..597
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 598..668
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 671..723
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 764..1021
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 419..481
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 714..755
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1024 AA; 116817 MW; 3562E3259C477A6D CRC64;
MIEFMKNGLA QRRLYLKPPR FNLKGTNIFV FLGLTLAGFF GNYFSIPLFF GVDFLFGSIT
ILLIAYCFGA RWATLAAVIV NLYTIILWGH PYSMILLDLE VLWVGLGLRR SSLNLVPLTC
LYWLVVGVPL GLIIYVFILQ LPNQLIALVI LKLIVNSVLN ALIASLVIFN SPFLSILDKK
YQRNYTFRQA VFNGLLAFTI IPVLLLIIVG SRAQFENLES QAIQAVSTLS EEFTENLKIT
REYRWGDLNL FEALIEAKRS PYPINVFLLN EYSVVKSYPE NAEIFDLGSG LMENKGNDVY
QWKPGGSMAV MTQWQQSYYY TIVNQPGLPW QILISLPAKP IVTQVQQFYI RNLAVVLGIM
GVGVICANTI SYRMIQPLTQ LTEVSSNLPE KVSSEEPWEL PNTNILELTL LSMNFEVMAN
ALRDKFKEIK QTNEHLEQRV SERTQRLAEI NHTLAAEVQE RKRIEAEIRQ SQQRLALMVE
QTPLAVMEWN MKFEVVAWNP AAERIFGYTA EEAIGTPIAD RIVPAEWKDH VSQVMAELIQ
EKQGVRSTND NIRKDGQRIV CQWYNTPLID EEGQCIGIAS MIQDITERQR AEMELRESEQ
RFRDVSEAAG EYLWEIDLDG CYTYLSERVV DVKGYAATDL LGRSPFDMMY RGDRDQVQHI
LEQATTEQST FQLEHRDVTP DGEIVWEEVN GVPRLDERGH LIGFRGAALG ITDRKRSELE
LRRSEAQLRQ KAQELETALR ELQQTQSQLV QSEKMSSLGQ LVAGVAHEIN NPVNFIYGNL
THAEEYVEDL LAVIASYQQH YPEPVEPVQE ELEASDVEFL VEDFPRLLNS MREGAKRIRE
IVASLRNFSR LDEAESKQAN LHEGIDNSLM ILQSRLKEKS HRSAIDVIRE YGEIPRIDCY
PGQLNQVFMN ILANAIDALD ERDRDRRPEE IREQPSCIWI TTQQQGDRVL ISIRDNGNGI
PEQIRDNIFN PFFTTKPVGK GTGLGLSITY QIIVDRHRGK IDCHSSLGEG TEFAIELPLT
PPPQ
//
