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Database: UniProt
Entry: A0A3D9KH14_9BACL
LinkDB: A0A3D9KH14_9BACL
Original site: A0A3D9KH14_9BACL 
ID   A0A3D9KH14_9BACL        Unreviewed;       610 AA.
AC   A0A3D9KH14;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DFP98_104157 {ECO:0000313|EMBL:RED85452.1};
OS   Cohnella phaseoli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=456490 {ECO:0000313|EMBL:RED85452.1, ECO:0000313|Proteomes:UP000256977};
RN   [1] {ECO:0000313|EMBL:RED85452.1, ECO:0000313|Proteomes:UP000256977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7287 {ECO:0000313|EMBL:RED85452.1,
RC   ECO:0000313|Proteomes:UP000256977};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RED85452.1}.
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DR   EMBL; QRDZ01000004; RED85452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9KH14; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000256977; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RED85452.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          331..384
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
SQ   SEQUENCE   610 AA;  69613 MW;  4A6E6E6E973D852D CRC64;
     MFPDSLIKRF HRTSFRNKLV LTYVLLIVIP VFSALFIYGT QLYRQTTTYY EDILEQLNQR
     TNVTIDDFFT NLARNSFFYL TDTKLHNIMD KALPSSDKQY LSDSNYMQNA MEQFVLINGN
     ISMIYVQAPN GSLYGSKSDK ANQLLDTLKE IGREKLRESK MYIHVPKAFD MNRNSGNQSI
     SIVRYLSDLN LNNGREAYAQ IDIYYKSIEN MLGGISVGDQ KLRTIVLAGD RVIYNSDGRS
     RIQSASDNEE LIAGLAKMKL TQEGSIVSNL RWNGEHYMVS GSLNRVTGWT VLQFIPSDRI
     TNTFIGNTVS YALFGILALI AALALAFFFH RYFANPILKL SGAMKMVDTG NLHNVTVKTD
     REDEIGRLIM SYNAMIERLK SSRASEIAAG QQQKKAELKM LQAQINPHFL YNTLNAIHSI
     SELHRIDTIS TMTKSLSSLY RYNIKYGDEV TVAKELEQID NYVKIQQIRF LNRFQVEYRV
     DPEVLSYKIL KFLMQPIIEN SFYHGLEPKG GQGLLTLTIK RQGQFLHIEV KDNGAGIAPE
     KLAELTAILE EDGAATGEDA DSGRHFGLRN VHTRIKHFYG DGYWMRVHSR EEEGTTIEMN
     IPLSKEDERP
//
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