ID A0A0P0C1I0_9BACT Unreviewed; 973 AA.
AC A0A0P0C1I0;
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=DC20_06840 {ECO:0000313|EMBL:ALI98732.1};
OS Rufibacter tibetensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALI98732.1, ECO:0000313|Proteomes:UP000061382};
RN [1] {ECO:0000313|EMBL:ALI98732.1, ECO:0000313|Proteomes:UP000061382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1351 {ECO:0000313|EMBL:ALI98732.1,
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; ALI98732.1; -; Genomic_DNA.
DR RefSeq; WP_062543145.1; NZ_CP012643.1.
DR AlphaFoldDB; A0A0P0C1I0; -.
DR STRING; 512763.DC20_06840; -.
DR KEGG; rti:DC20_06840; -.
DR PATRIC; fig|512763.3.peg.1512; -.
DR OrthoDB; 9766459at2; -.
DR Proteomes; UP000061382; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000061382};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..294
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 336..389
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 407..458
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 459..529
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 532..584
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 740..954
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 973 AA; 110151 MW; 68C2E3DFC7C70909 CRC64;
MIFSRLKDYY LALGSFMLVL GITIYAYYVS KANDQTEDAQ EFKIKQVQIK ATLERRMGYY
LQILKGVNGL FAATDTVTRE DFQSYLKSLN ILESYPGVQG IGFTVMVTPE ELPKLEERIR
AEGYPNFKVH PAGQRTEYSA IIFLEPLSRQ NLRAFGFDMF NDPTRREAME AARDSNLPAM
TAKVKLVQEG QKNVQPGLLI YLPVYYGGVD PGEGNRRSML KGFVYAPFRA GDLFSKTIDS
SHDDISISIY DGKEIKEEAL LYRNAAKVEV SESSDSLLLA TDMIRFAGRT WTIRYKATRA
FAEASGIDQH DLILLGGCII SLLIFFVVWS LQRYLRSNQL TELITKNTTA GLFMLDDRGY
CTFQNPSAER LLGYSLDELK RRPLYELVHK GQEPGNLAPE LVSQKAFTFE DSFVCHDGNL
IPVACSTRFV KQGGEVVGHI LEVRDVTEEK KAQQALLESE ARFRNMADSA PVMIWITDEK
DNCTYVNRQW LKFTGSNLDE NMGLGWLKFV HPDDTQTMTQ AYKQALSEKS ELKVEYRLRR
RDGDYRGVVT MGIPRFNAED EFLGYIGSSI DISDRIKMEQ KLKQSADTLQ RIFMQVPAIV
GLVRTKDLRY TLVNSYLSSL YEGKAQVGVI ATETFPESQR EQFKNVIQHI VDTGEPFIGQ
EVPVSFDDSE EGQKNIRFFN IVYEPIKNSG GEVEFVLTFA VEVTEQVKSR EQLSTINEQL
NDKNQELIRI NNDLDNFVYT ASHDLRSPLA NLEGLTTALL ETVEGKEEGE EHMLLHMVVS
SIAKLKGTIH DLTEITKVQK DLDSQAEVLS FAEVLAGVEE DIAGMIQEAG VQLNTSFQVK
TLRYARKNLR SILYNLVSNA VKYRDPSRKP QVTLTTTRQD GFVVLTVQDN GLGIREDQQE
KLFTMFRRFH SHVEGTGIGL YIVKRIIENN GGRIEVNSEP GRGTTFTVYF RENPLVPAPV
DVASKEEIEE TKG
//
