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Database: UniProt
Entry: A0A0K8JCJ1_9FIRM
LinkDB: A0A0K8JCJ1_9FIRM
Original site: A0A0K8JCJ1_9FIRM 
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};
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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
//
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