ID A0A0X8XCB9_HALHR Unreviewed; 412 AA.
AC A0A0X8XCB9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HH1059_11850 {ECO:0000313|EMBL:BAU57879.1};
OS Halorhodospira halochloris (Ectothiorhodospira halochloris).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=1052 {ECO:0000313|EMBL:BAU57879.1, ECO:0000313|Proteomes:UP000218890};
RN [1] {ECO:0000313|Proteomes:UP000218890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-1059 {ECO:0000313|Proteomes:UP000218890};
RA Tsukatani Y.;
RT "Halorhodospira halochloris DSM-1059 complete genome sequence.";
RL Submitted (FEB-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP017372; BAU57879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X8XCB9; -.
DR KEGG; hhk:HH1059_11850; -.
DR OrthoDB; 5777124at2; -.
DR Proteomes; UP000218890; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13188; PAS_8; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000218890}.
FT DOMAIN 3..44
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 83..135
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 229..281
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 278..315
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 128..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 46092 MW; 4D4D0B80C1F48162 CRC64;
MEAKEFYNNM LDRCPAGVCA LDVAGYFTYL NSEACELLGY PDAEQLLGRS FDTVVDYYSQ
LPQRFTVADR LALVAATQED IRCYEPVRLK KNNAEPFAVS IDASPLRDDK SAVIGVILVL
RDVMERRRQS NTAPHRENDT PLHEDNHSSK KCELELSEPQ RLAKIGLGSW VWDLRTGYTF
SSTEVYRSIG VEKAAFDPSQ KGFLAVIHPD DQQAVEAEFE QALRDQQPWA SEYRILPANG
DVRIVLERGH FETDDLGKPL RIIATVEDVT EQRKEENYQK QLIDILDNTS DVVALHDYEG
KMIYVNTAGI ELVGLGAGIY NNNADQNSPE LPESVEDSIL RFHPQWAADL ILNEGVPTAL
SEGIWHGETA LLNESGEEVP TSQVIIGHRD ASGEVVQFST VLRQIPKTRA NG
//