ID I4Z9Y8_9BACT Unreviewed; 565 AA.
AC I4Z9Y8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PrebiDRAFT_1319 {ECO:0000313|EMBL:EIM33030.1};
OS Prevotella bivia DSM 20514.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=868129 {ECO:0000313|EMBL:EIM33030.1, ECO:0000313|Proteomes:UP000002786};
RN [1] {ECO:0000313|EMBL:EIM33030.1, ECO:0000313|Proteomes:UP000002786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20514 {ECO:0000313|EMBL:EIM33030.1,
RC ECO:0000313|Proteomes:UP000002786};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Munk A.C.C., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Improved High-Quality Draft genome of Prevotella bivia DSM 20514.";
RL Submitted (FEB-2012) 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; JH660660; EIM33030.1; -; Genomic_DNA.
DR RefSeq; WP_004336050.1; NZ_JH660660.1.
DR AlphaFoldDB; I4Z9Y8; -.
DR GeneID; 78531291; -.
DR HOGENOM; CLU_000445_89_2_10; -.
DR Proteomes; UP000002786; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EIM33030.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002786};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 166..218
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 227..275
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 349..565
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 565 AA; 63524 MW; 09D8A412FDD466BB CRC64;
MKIKTKISSL FGLLLGTILL MGAFACITVY QQKVSTERIL KDNYHSVTYA QQMLSATNIY
YTDSVNSLKN FRENLALQKK NVTEQEERMM TERLESRFNA FLAQPTTTNM LQLHEAINTI
IRLNTNAIYY KSEQASDSAK TALLWTILMA LLCAGVATFM QIHFPKSLSS PIQKLIEGIT
EIANGHYGKR LEFAEDAEFA PVATSFNHMT EQLALYEESN MARIIAAKQY LETVVRAINK
PILGLNQQQE ILFANTALSN LINLPEDKLV GQSALALSVN NDLLRRLVKG MPENGGSEKE
PLKIYADNKE SYFEVHYLKL ADEYGTVVML NDVTKFKELD NAKTNFISVI SHELKTPISA
ILMSLQLLED KRIGTLSDEQ QELAKSIGDN SDRLLKITGE LLKMTQVESG SLQLSPKVTK
PIELIEYAIK ATHVLAERFE CNIEVEYPTE KMPKLFVDSE KIAWVITNLL GNAIHYSPQH
GRIIIGARQT ENRIEIYVRD FGKGIDPRYH DTIFERYFRV PGTKVQGSGL GLAISKDFVE
AHGGNIRVES EIGKGSCFIV TLDSM
//
