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Database: UniProt
Entry: A1WTU3_HALHL
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Original site: A1WTU3_HALHL 
ID   A1WTU3_HALHL            Unreviewed;       639 AA.
AC   A1WTU3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Hhal_0311 {ECO:0000313|EMBL:ABM61105.1};
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM61105.1, ECO:0000313|Proteomes:UP000000647};
RN   [1] {ECO:0000313|Proteomes:UP000000647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA   Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABM61105.1, ECO:0000313|Proteomes:UP000000647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RX   PubMed=23991253; DOI=10.4056/sigs.3677284;
RA   Challacombe J.F., Majid S., Deole R., Brettin T.S., Bruce D., Delano S.F.,
RA   Detter J.C., Gleasner C.D., Han C.S., Misra M., Reitenga K.G.,
RA   Mikhailova N., Woyke T., Pitluck S., Nolan M., Land M.L., Saunders E.,
RA   Tapia R., Lapidus A., Ivanova N., Hoff W.D.;
RT   "Complete genome sequence of Halorhodospira halophila SL1.";
RL   Stand. Genomic Sci. 8:206-214(2013).
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};
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DR   EMBL; CP000544; ABM61105.1; -; Genomic_DNA.
DR   RefSeq; WP_011813128.1; NC_008789.1.
DR   AlphaFoldDB; A1WTU3; -.
DR   STRING; 349124.Hhal_0311; -.
DR   KEGG; hha:Hhal_0311; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_15_6; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000000647; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
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; 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; 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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
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; 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; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABM61105.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000647};
KW   Transferase {ECO:0000313|EMBL:ABM61105.1}.
FT   DOMAIN          136..190
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          214..264
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          275..491
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          518..637
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         567
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   639 AA;  70545 MW;  E6F284B796336C2F CRC64;
     MTEPSRYGWD DAINAVHSLV FLHDGDYRIL RANRAYLEWA GASTEEEVIG RPYWEVFPRG
     DGPLPACRRA MEQLGAGSPQ AGDGVESSEE IELPSGEIFR SRSYTVREAD GSYRCSVHIL
     EDITEQRRLE QARQGAEAKV KAIAAAARDA IVLIDDDDRL VYCNAAFEAL LGYEAGELVG
     SPFHEQVAPS RYRTSARTGM RRFRVCGGGA VIDQRTEIEA LHRDGHEVPL ELSVSPLQLD
     GRWHAVGVMR DISERRALEV DRQRAEADRN IFLAAISHDL RTPLNAIVGF TDLLARSELD
     TEQRHHVGLC RSASQTLLGL IDTVLELSRL EAGRVELRDE RFNLPAFLTT QIGLLQPMAE
     EKGLSLIWSL EPDMPGWVRG DPVRFGQVLY NLVSNALKFT ETGSIRVDGA RSTCGRLMFT
     VADTGPGIPE ADQGRIFDAF CQGGPVLARK EGSGLGLKIC QELVRLMGGT IQLVSTPGVG
     TTFRFTVTLP SAEPDRAEAA AVPQEAVDTE APVGQGLWVL VAEDDPTNAL LFQKLLEQAG
     CHVTVVGNGR EAVRHWQRAS PDLVLMDLQM PEVDGREATR RIRAREAEDW LPRTPIALVT
     AHALDSFQQE CFRIGCDAYL TKPLDRAELW QLLARVRAA
//
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