ID Q2S5A3_SALRD Unreviewed; 1346 AA.
AC Q2S5A3;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=SRU_0483 {ECO:0000313|EMBL:ABC46267.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC46267.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC46267.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC46267.1; -; Genomic_DNA.
DR RefSeq; YP_444628.1; NC_007677.1.
DR STRING; 309807.SRU_0483; -.
DR EnsemblBacteria; ABC46267; ABC46267; SRU_0483.
DR KEGG; sru:SRU_0483; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR OrthoDB; 1489484at2; -.
DR Proteomes; UP000008674; 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; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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; PF00072; Response_reg; 2.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABC46267.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008674};
KW Transferase {ECO:0000313|EMBL:ABC46267.1}.
FT DOMAIN 825..1049
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1073..1186
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1209..1326
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1187..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 791..819
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1193..1208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1123
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1258
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1346 AA; 146886 MW; BF656E692EBA02E8 CRC64;
MQGSPSAVPR SDDFVWMLHS AVKRYGIRLA CGVVVGALLL SSPAAAQNKR ITAYETEDGL
PEMQVWDGLQ GPEGYLWLGL YGGGLARFDG QEFKRLTIDE GLPGNLATTV HTDSTGVIWV
GTLSGLARYD GREMTTLTAD NSALVQNGIQ SIVGGTNGTP VWVGTSDNVY VHDGEGLRQL
APDRLQNLYP DGLASRGDTL WVGTSNGLYR YTDSTLTALS VVDGGATASV TTLAAPPSGR
LWVETGQGLF RRVGSRFEKL PGTSDRDVLS ILDPSGRAPW LGTRSGLYRW RGGRLQSTAI
GDVSVQGLFE DQEQNVWVTT DSEGLYKYPH TPFDHFSTAD GLPGDVSWDV DRGPNENLWI
ATRNGLSRYD GTSFTDVPGP DDQLRQELTS IHWTQDDILW IAARSTLFRY DGDTYTSYDR
VEGDPVGTVT RIVETPSGTL WFATTERGLL RYDGSGFARF TTADGLTSDQ VRSVTVDDTG
QVWAGEGASR FDGASFHPTP AVDSADLGGV LSLEVDAKGH LWIGTQRGVF VHPPPQRGEA
ASLRRITPDD GLNGTSSVNL HLDRHNNLWV GNEGGFNRID VDAYHRTGQV SIRSYDKDVD
LRGGVATEHA TYEADGGMLW FGTSTGLVRY NPAQDRGRPA PPQTHLTDIQ LYPEDPDWSR
YADGTTPWEQ LPTNLSLPYD KDHLIFRFIG INYTVPERVA YRYRLEGLDE RWSTATKRQR
ATYSNLPPGS YTFQVQAANS DDVWGPVEAY SFTITPPFWR TTWFYLLCAI GGIGLVTGLI
RWRTWSLQRR QRLLEAKVAE RTEELEEARE EALAAAEAKS KFLANMSHEI RTPMNGVIGF
ADLLSDTDLT PEQQQFVDAI QSSGTTLLSI IDDILNFSKL EAGETELEEA PIRVQTCIEE
ALDPLAAKVA EKGIELTYLI DPAVPSVIRG DRTRLHQILL NLLSNAVKFT EEGEVALRVR
VASSPATPDG TYELHFSVRD TGIGIPKEKR DRLFESFSQV DASKSREHGG TGLGLSISQQ
LTEAMGGEMW VESAVGEGST FHFTIEAEEA EDGAQTDKNG VATGSSSAMQ GVQVLIVAPN
DTNRALLRQQ TETWGMEATV FASGDEALQQ LDADRAHEVA LIDEHLPQMS GHALATQLRE
RASGTELPVV LLGAGPAATP DLTAPTSRLH KPIKQSSLHD TLTALLTGRE NGGSGRDGDR
SGPDSPSRRV LLAEDDAVNR TMTTQLLEKM GHEVYTASDG AEALAAVRDQ AYDAILMDVQ
MPELDGLEAT RRLRNEMPSE EQPYVVALTA SVTEDDRRRC LEAGMDAFLS KPIRKDELAE
ALDLGTAPDE ARTAAPPPED HSAPDA
//
