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Database: UniProt
Entry: A0A3E2J4V5_9BACI
LinkDB: A0A3E2J4V5_9BACI
Original site: A0A3E2J4V5_9BACI 
ID   A0A3E2J4V5_9BACI        Unreviewed;       598 AA.
AC   A0A3E2J4V5;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=D0463_15720 {ECO:0000313|EMBL:RFU61003.1};
OS   Bacillus sp. V59.32b.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1758642 {ECO:0000313|EMBL:RFU61003.1, ECO:0000313|Proteomes:UP000258625};
RN   [1] {ECO:0000313|EMBL:RFU61003.1, ECO:0000313|Proteomes:UP000258625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V59.32a {ECO:0000313|EMBL:RFU61003.1,
RC   ECO:0000313|Proteomes:UP000258625};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT   sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT   Center where the Viking Spacecraft were Assembled.";
RL   Submitted (AUG-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:RFU61003.1}.
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DR   EMBL; QVTC01000073; RFU61003.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E2J4V5; -.
DR   Proteomes; UP000258625; 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:RFU61003.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000258625};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          320..372
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
SQ   SEQUENCE   598 AA;  68627 MW;  4DDC0929DEBF64BA CRC64;
     MWKFRYKGLQ AMKDVLRTMI KFLDSSIKRK MIVMVVVTLI FVVGMIDIVT YGVSINLQMN
     DAKANDARKV QFVIENIDET ISNMSSLMDS ISQDAEIQSM LSNSSVISVS NLEKIIFSKT
     SYSSNIFEHL YLYDNQKLII KLNFNSGNKT NRNMINQTTF NKYRFDTVGR TSWRIENGVI
     YIDKAIRQRE SLKILGYITI ALKEDYMKQR LQSEEYRYTY VFNENGDVIV SSNKIAELNL
     DELYSRAKQE PNGIPTQLNI KPFGKMIFTT NISEFGKWRV VSLVPVKEIA KGPELIGWWI
     MIIGFLGILV GIIITWKGTK RLIAPLYQLK QVMDQVETGY FKQNVNIQSN DEFARLGRSF
     NRMMEEINHL ISEVYQKELS QRESEYKALK AQINPHFLYN TLDTIRWLAL YGESKKIEKV
     AISLAHLLKA SLKESKEMIP IKTEMEYINA YLFIQQTRFE KINVSIYLDE DITNFFIPRF
     ILQPLVENSF IHGLEKKVGN GNLIISGSVS HQSLTIRVID NGVGMNQEEA QLLLSAKEDE
     HIDIAKGTGK GLKNVNKRIQ ALFGEEYGLS IQSSLDTGTI VEIMLPAIKH SIMTSKSI
//
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