ID A0A0P0CUH9_9BACT Unreviewed; 2049 AA.
AC A0A0P0CUH9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DC20_02235 {ECO:0000313|EMBL:ALI98009.1};
OS Rufibacter tibetensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALI98009.1, ECO:0000313|Proteomes:UP000061382};
RN [1] {ECO:0000313|EMBL:ALI98009.1, ECO:0000313|Proteomes:UP000061382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1351 {ECO:0000313|EMBL:ALI98009.1,
RC ECO:0000313|Proteomes:UP000061382};
RA Dai J.;
RT "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT radiation-resistant bacterium from tibet plateau.";
RL Submitted (AUG-2015) 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};
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DR EMBL; CP012643; ALI98009.1; -; Genomic_DNA.
DR RefSeq; WP_062542335.1; NZ_CP012643.1.
DR STRING; 512763.DC20_02235; -.
DR KEGG; rti:DC20_02235; -.
DR PATRIC; fig|512763.3.peg.502; -.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000061382; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd19410; HK9-like_sensor; 1.
DR CDD; cd00130; PAS; 6.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 3.30.450.20; PAS domain; 10.
DR InterPro; IPR007891; CHASE3.
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; IPR036641; HPT_dom_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; IPR013655; PAS_fold_3.
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 NCBIfam; TIGR00229; sensory_box; 8.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 4.
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; 9.
DR SMART; SM00091; PAS; 9.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 10.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 6.
DR PROSITE; PS50112; PAS; 6.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000061382};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 229..299
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 362..432
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 616..656
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 694..746
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 822..874
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 875..947
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1077..1129
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1130..1184
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1208..1258
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1333..1384
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1392..1444
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1467..1519
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1537..1759
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1786..1902
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1943..2048
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 1510..1537
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1836
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1982
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 2049 AA; 232804 MW; EDFD3FA97941D021 CRC64;
MPDTYRALNK IKNFKRLLTG LLSGLIFSGI LIYGAYYNLN REKEISQWTL HAQEEIYQIE
RTISLVKDFE TGSRGVLLTN KDEYEQPLKE ASKNLSKVLA HLKKLSSDDL IQKSHYDSLF
FYLNQKVAFS TSVIRLRQEQ GPKIALQLFQ TNEGLEYMDK IRHFADLMLL HEKDVLEQRK
MESEKASSLT NLILSCSLLF FVLLLMYMVY KGWKQENEKE KAVQKLKERE EHFRALIENN
SEAIVLKDIK ESIIYWSPGA EKILGWTAEE AAQPGFSTLV HPEDRKRIQL QKEQIAANPS
LPVKGTQRVL HKNGHYVWIE GETMNLLHQS SVHAIVSNFK DVSDRVAADL KVQEAHALLE
KSVSNLNQIM DSSIDVICTI DALGRFAQVS AASAAVWGYP HEELTGKAFM DFVSDQDKEL
TKVVAISIMA GNPVTTFENY YVRPDGSLVP VLWSAQWSEK DQLMYCIAKD ATEKKKLEKA
FHLEQQRFND LFMQAPSAIC VLKGADHRFV SSNPLYNQLV GSNRIILGRT AQQAFPELID
QGFLTLLDQV YTSGEPFIGK EQLIQLDKEG NGNLTDIYAN VVYQAYTNSL GEVEGIYFFG
VDVTEQVLAK KKVEESEGNF RKLIEDLPAA VYTCTTDGQI KLFNRAAVEL WGREPETEKD
LWCGSWKTYD CNGHSLALED SPMAATLKHE KPALDQEIII ERPNGERRYV KPHPVLSYNA
AGDLIGGINI LTDITESKNA SEQIRRSETA LAEAQRIAKI GSWSMDLLTQ DLSCSKELYK
VFDTDKEQFT GTFTSFLAFV NESDQANAWD TTYKAAYDGK PFEVEYNITT GKGENRIIHV
IGSTQADDQG EVVRLFGTAQ DITERKEFEN ALLASEEKYK LLFYQAPLPK WIYDLETLRI
LDVNESAIMH YGYSREEFLQ LTAQDLRPEE DVPALLNSLL NEETGKGVYR LGLWNHLKKD
GTLIKVEISA HALDYENRNC LLVEANDVTE KVKAEQAVKE SNNRWEMLSK VTFDAIWEWD
LKSNELICGV NYKTLFGQNL SDNKEDYQAW DFYLHPDDRQ RVNESLKAFL KSGESTWQEE
YRKLNSKGEY AYCTDRAILI RDGHNEPVRM IGALRDVTES KLAAENLLIE KNFSEALLEA
TPDGIVGFNE KGEIIIFNKK AESLFSYTQE EIIGASLTKL LPSDTHVAHL DRRENFFSNP
TESQLQASSR EMIGVRKNGS EFPVDVRLNL LHSYKGRIVI SSIRDITQRK RAETQLRESE
KNLKAILSSS QEGIYLLDTN CQLVLLNEHA QDIILRGYGV NCKPGDHFPS LFDTELNGKL
EVIFEKVLAG DKWESERNIP LLEGMAHYHS VYFPVRDKEG NIIGICCSSK DITEKKKIEE
AIKVAQAEKE EYQYRFKAIL DYSPQAILIK DLEGKYIFSN KAFLKLFDLD RNNEVGQQLK
EVFEDQITRA EFLANAPEVD SDIILTKEWS QQIHLPDGNI LDMEILKFPL YDQQKRLFGI
CTICKDITEQ MKHQQQLIEA RENAEQAERL QEQFLANMSH ELRTPMNGII GMVNLLLTSS
SLQPDQKGRL QVIQRSSDTL LSLINDILDL SKIKAGMLTI DKVNFDFNES IAGTALLFKE
KAKEKGIKLT VTSNPFIPRL LAGDPHRLNQ ILNNLLSNAI KFTEKGFVRL EASLQSETED
QVVVEFVVSD SGIGMEAANL LYIFDNFAQA STDISSKYGG TGLGLAITKR LVEMQGGEIS
VASTKGIGTS FTFHLPFSIT QDTNMVVKPY YQTAHVPLKK DYSGKRALIV EDNDINQAVL
ASSLKQHHMD LQIANNGQEA IDLLETGEHF DIIFMDLRMP VMNGFQATAY IRQKLHKQVP
IVVLTASVLR NERNRCLEIG ASDYMAKPFA MADLARTLEQ FVSKEEQISE PATEPIITTD
TPFLSHAQQG AEFDISRLME LEDPEYIRHI FTLFTDKVPT YLQELKNNSL NGNWEDFLEK
THKIRGSLSS VQIDEIYGLI LSIEEKVREE KTLSGLEHQL DKCLSIYNQL IPSIYQEVEK
QLVPLEADL
//
