ID A0A0K8JCJ1_9FIRM Unreviewed; 921 AA.
AC A0A0K8JCJ1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=P22_1290 {ECO:0000313|EMBL:CUH95220.1};
OS Propionispora sp. 2/2-37.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Propionispora.
OX NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH95220.1, ECO:0000313|Proteomes:UP000041641};
RN [1] {ECO:0000313|EMBL:CUH95220.1, ECO:0000313|Proteomes:UP000041641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2/2 {ECO:0000313|EMBL:CUH95220.1};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CYSP01000005; CUH95220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K8JCJ1; -.
DR STRING; 1677858.P22_1290; -.
DR Proteomes; UP000041641; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.12370; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000041641};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 681..897
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 921 AA; 102077 MW; 912CD0CFEA6ECE8B CRC64;
MMVQEADKRP DPEELLQKIH KENRGKLTVF LGAAAGVGKT YTMLEAAHDR LAEGVRVVIG
WVETHGRAET EKMVAGLPRI APKMLEYRGR QLPEMDIDAI MNKKPELVLV DELAHTNING
SRHVRRFQDV EELLNAGIHV YTTLNIQHIE SLNDVVVQIT GVFVRETVPD LFIEQADNIQ
LIDIPPEELI KRLKDGKVYV PGQAEQALKK FFRPGNINAL RELALRFTAS RVDQDMAEYM
REHRIDGPWP AAGRVMVCVS ASPFSAQLIR AAHRLASGLR ADFLAVYVDT PVRRFPMGER
EKDRVWRNLR LAEELGGKIV TVIGSDIVQE MLTVARGENV TAIVIGKPRH SRWREFWHGS
LVDKLIRHSE GINVYVIQSN AEAEVRSPIS TALPASAAVP WMFIAGGCLM TAAVTAASWL
GRRQLELVDI ALLYLLPVLF SALWWGRWPS YITAMVCILA FDFLFIAPVM TFAVSDIRYL
WSFIIFLIIS FVIGGQTEML RREVRLTRQR ETSVRTLYNF SRQIAAVIDV KQIAWKFVSH
TGMAFDRNVV MLLPAENGKL AVAGTYTAGL PDGQAGRAQL PAAEYAVASW AFVNGQVAGR
STETLPGADY LFVPLLADGR TVGVFGIELG QQKITQEERQ LIYAWVGLAA VAVERVKLSE
VARQAALLKE SDQLRTALFN SVSHELRTPL AAIVAAVSTL LDAGVKYSAE LQRELLETVQ
DSASRMERVV ANLLDTARLE SGMLHLKTDW CDIEDIVGVS IRRMGDTVKK HFLKTRLSPK
LGLLRADCVL LEHVLVNLLD NAVKYSPPGS EIIIAAEPYG REIIVSVQDN GPGIPVQDIK
KIFEKFYRVQ HQTVKIAGTG LGLSICKSII EAHGGRIWAQ NAPAGGAIIS FAVPVPDENS
RTLVKAGESN DGTGTAYSDH R
//