ID A0A0P4V2I3_9CYAN Unreviewed; 963 AA.
AC A0A0P4V2I3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES2104_54100 {ECO:0000313|EMBL:GAP98854.1};
OS Leptolyngbya sp. NIES-2104.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP98854.1, ECO:0000313|Proteomes:UP000052243};
RN [1] {ECO:0000313|EMBL:GAP98854.1, ECO:0000313|Proteomes:UP000052243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP98854.1,
RC ECO:0000313|Proteomes:UP000052243};
RX PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA Kawachi M.;
RT "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL DNA Res. 22:403-412(2015).
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:GAP98854.1}.
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DR EMBL; BBWW01000001; GAP98854.1; -; Genomic_DNA.
DR RefSeq; WP_059000862.1; NZ_BBWW01000001.1.
DR AlphaFoldDB; A0A0P4V2I3; -.
DR STRING; 1552121.NIES2104_54100; -.
DR InParanoid; A0A0P4V2I3; -.
DR OrthoDB; 2079555at2; -.
DR Proteomes; UP000052243; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:GAP98854.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:GAP98854.1}.
FT DOMAIN 2..107
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 427..661
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 663..805
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 840..957
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 890
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 963 AA; 107063 MW; CA8002694A153DF4 CRC64;
MKQDRELEIR RQFLDEAQEY LDTLDATILG VSNHPIEASK ANAALRAAHS IKGGAGMMGF
QVLSELAHRL EDSWKVLKID KSVTVTPRLE NLLLAAVGCL RQVVEFDRDS LQRHQASCVD
ANWLSVEAYP VFDALHSELG DPQEENAASV LSPEDGQDIV PLLFETEVEG CLQRLEAVLA
TPEQPCLREE VSILAQELGG LGEMLQLTNF IQLCQSVSHQ IEDESADTIE LAESALKFWR
TAQMFAIAGQ YDQIPMSIDG SVPELTDFAE TPSVLEPSMG DWFTEALDSI DEEGYTDFQP
IPAPARSAPP EAQVTDFKVL EAEPDPVPVA ENDDATVRVP VRQLNQLNDL FGELTIDRNG
LDLYLKRMRT LSRTLHERVQ VLDQVNSKLR TAYDRVTLVG QRALTDGSNR RAGFDALELD
RYGDLHLLSQ QVMETIVQLQ EVTEDIDLSL DDTDQAARNL NKTAKQMQSG LSQLRMRPIS
DILNRFPRAL REWSLQYGKQ IRFDMGGSGT LIDRNILETL SDPLMHLLRN AFDHGIESPN
VRESRGKSPE GIIEIRAANE GNRTVITVRD DGEGIPIDKI RDRAEQMGLD PVLLDAARDE
ELLSLIFEPG FSTSSQVTAL SGRGVGMDVV RSNLKQIRGE ISVHTEAGVG TTFTLSVPFT
LSTVKVLLVE SAGILLAFPT DVVSELFLLQ PHQVIQTPGS EVLNWQDHMV QLVRLQKWLR
FNCPRIPHGF ETPPTIASQS VIILDQNPQW FGIHIDRCWG EQEATIRKVE GNLSLPTGFS
GCTILGDGRV VPLVNVAELL RWITSCERSE AQPSTENAFR DQLRANLTQR PELPGSSTPT
VLVVDDSINV RRFLALTLER SGYRVEQAKD GQDAIERLEA GLSVQAVICD IEMPRLDGYG
FLAKLRSDGQ LSQLPVMMLT SRSGEKHRKL AENLGASAYF SKPYNEQVLL RTLESMVQST
VTV
//
