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Database: UniProt
Entry: A0A0F5R6M2_9BACL
LinkDB: A0A0F5R6M2_9BACL
Original site: A0A0F5R6M2_9BACL 
ID   A0A0F5R6M2_9BACL        Unreviewed;       578 AA.
AC   A0A0F5R6M2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=VE23_18200 {ECO:0000313|EMBL:KKC48571.1};
OS   Paenibacillus sp. D9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC48571.1, ECO:0000313|Proteomes:UP000036611};
RN   [1] {ECO:0000313|EMBL:KKC48571.1, ECO:0000313|Proteomes:UP000036611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D9 {ECO:0000313|EMBL:KKC48571.1,
RC   ECO:0000313|Proteomes:UP000036611};
RA   Sharma V., Lin J.;
RT   "Genome sequence of surfactant producing, diesel degrading Paenibacillus
RT   sp. D9, isolated from diesel contaminated soil.";
RL   Submitted (MAR-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   -!- 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:KKC48571.1}.
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DR   EMBL; JZEJ01000001; KKC48571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5R6M2; -.
DR   PATRIC; fig|665792.3.peg.4037; -.
DR   Proteomes; UP000036611; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; IPR005467; His_kinase_dom.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000036611};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        286..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          306..358
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          467..571
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          346..380
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   578 AA;  66330 MW;  7F82FD9D6B5DBEC8 CRC64;
     MRMLRSRFMF SSLRKRIMVF LTVGLVGCAV LMASVSYNAI YTMQRDKIKT SMAFDLHQQT
     SKVNQMYSSL LQVSQQMTPE GTVGNLMETY ISATDIYSQR LLSRDISYNI GLITFSNPAM
     ELVMYYNPAT GNASYSNLPL RSGFTRQSLP DVAGMGELKY QSPHKSLCRF SDDQVVSVTR
     EIRFSDGTQL VVYVEAKSDL ITDMNSLAES LNIPYTLVFT DSKDAVTYSS NSTAYAVGQR
     LRLSGQSGMT DGYVWNRMKG EYGYDITLLL PVSSYNHELY TWKNHMYWIL AVALLMMFML
     TLLLRRLINR PFLMIEKEMR TFGKGYMGTS RYHTGIDEFD RIFDQFNVMK RQIQQLILDV
     EQKEKRRHQL EIEKLAYQIN PHFLMNTLNS VRWLAVMHKQ AEIEKFVSSL IFLLSYNLGK
     SEERATFRSE IDVMRTYLEL QQMRHDFEVK LAIAEGTYLD SSVARFILQP IVENAVCHGL
     DDNGKLEISI VPDETAQMVR IVIRDDGKGL SRETLALLQR DTPDQQQTGW GIGLRYVRSM
     LESFYGYKAR MGIESTPNQG TTVTLELPVL HPRKESAS
//
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