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Database: UniProt
Entry: F4C8H2_SPHS2
LinkDB: F4C8H2_SPHS2
Original site: F4C8H2_SPHS2 
ID   F4C8H2_SPHS2            Unreviewed;       396 AA.
AC   F4C8H2;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Sph21_3863 {ECO:0000313|EMBL:ADZ80397.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ80397.1};
RN   [1] {ECO:0000313|EMBL:ADZ80397.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ80397.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) 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; CP002584; ADZ80397.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4C8H2; -.
DR   STRING; 743722.Sph21_3863; -.
DR   KEGG; shg:Sph21_3863; -.
DR   PATRIC; fig|743722.3.peg.4122; -.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3706; Bacteria.
DR   HOGENOM; CLU_000445_114_72_10; -.
DR   OrthoDB; 9781208at2; -.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ADZ80397.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:ADZ80397.1}.
FT   DOMAIN          155..371
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   396 AA;  45424 MW;  E5B12337B05D7726 CRC64;
     MILVFDSLAE AKNSLMRILE ANSLPAQAAM STDETLQHIF TYKYKLLILR ADAFEGSDAQ
     EVLRVMNNNP NAKDTPVLLI TPSSIKQKIK FETYTGLWLD CLFGDYSTDF LIFKIKSIQD
     RQEYIAGLYH DNRFLKEELQ KTKMTEAAKE EFISIAGHEL STPITSINAY LQLALRNANS
     QNIEQTIQLL SKGLNQINKL NRLAKDLLDS SRLQAGKMEY NFAVFNCRDF LRQTTENVRH
     SYPDRQINVN CNTKVWLEGD QERLEQVLTN YLTNALKYSP TSTEVLVYTE IIDKKWLKVC
     VKDRGQGIPR EKQPYIFHKY YRVSDEKHKH QGLGMGLFIC AQIISHHKGK FGLESEPGKG
     SIFYFMLPIK ATKEKTEGLT TSFPKRSAFS SSNLNK
//
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