ID A0A2W1JM77_9CYAN Unreviewed; 683 AA.
AC A0A2W1JM77;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=walK_1 {ECO:0000313|EMBL:PZD74473.1};
GN ORFNames=C1752_00792 {ECO:0000313|EMBL:PZD74473.1};
OS Acaryochloris thomasi RCC1774.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris; Acaryochloris thomasi.
OX NCBI_TaxID=1764569 {ECO:0000313|EMBL:PZD74473.1, ECO:0000313|Proteomes:UP000248857};
RN [1] {ECO:0000313|EMBL:PZD74473.1, ECO:0000313|Proteomes:UP000248857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC1774 {ECO:0000313|EMBL:PZD74473.1,
RC ECO:0000313|Proteomes:UP000248857};
RX PubMed=29904088; DOI=10.1038/s41598-018-27542-7;
RA Partensky F., Six C., Ratin M., Garczarek L., Vaulot D., Probert I.,
RA Calteau A., Gourvil P., Marie D., Grebert T., Bouchier C., Le Panse S.,
RA Gachenot M., Rodriguez F., Garrido J.L.;
RT "A novel species of the marine cyanobacterium Acaryochloris with a unique
RT pigment content and lifestyle.";
RL Sci. Rep. 8:9142-9142(2018).
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:PZD74473.1}.
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DR EMBL; PQWO01000002; PZD74473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1JM77; -.
DR Proteomes; UP000248857; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR000253; FHA_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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:PZD74473.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248857};
KW Transferase {ECO:0000313|EMBL:PZD74473.1}.
FT DOMAIN 50..110
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 332..402
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 469..683
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 294..328
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 436..465
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 683 AA; 77427 MW; 521CF7BC4B0DB070 CRC64;
MHTQIIGGRP REKTRSSNVQ EREQQRPIHH LLLIEDQKGK RTVALEAATC TIGRGESNTI
VLVSETISRH HAILLRVTTP QAVTHQFRIV DGNLQGQRST NGISINSKRC YSHNLVHGDV
IIFGGNVMAR YFATSDPADI DFLTSCETDD MSGFLSGLHN PFETISGQVE DNEASLVRLA
SFPELIINPI IEVDSTGQIT YLNPAATRQF PDLPRQQQQH PVLAGLIERV QQNEDAFFER
EITHRDCIYN QSVHCLETSE LIRIYLIDIT EKKQTQAALH NSERRFREVL QKAHDDLEVR
VQERTTELEQ ANKRLISEID ERQRAEEALR SSYATNRALL NAIPDWMFRI SVDGTFVNYK
AANQETIPLP TDDFLGRTVY EVLPSEVAKP LMKCINEVLL EQEVKIFEYQ LQRNGSQTDF
EARIALSAEN EIMAIIRDIT ERKKAEQDIR NSLEKERELN ELKSRFVAMT SHEFRTPLAT
ILSSSELIEH YSHKWPEDKK KKHLRRIQVS VHHMTGLLND VLLLGKADAG QLQFQPIPIQ
LIEFCEDLVE SIQITTENHE IHFTHSGDFT DVKMDEKLLR HILGNLLGNA VKYSPLGGNV
YFDIQSLENN IIFKVRDNGL GIPKSEQENV FNSFNRASNV GTISGTGLGL AIVSKSIDLH
CGKIGFESQE GEGTTFTVEI PVN
//
