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Database: UniProt
Entry: A0A061P665_9BACL
LinkDB: A0A061P665_9BACL
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ID   A0A061P665_9BACL        Unreviewed;       522 AA.
AC   A0A061P665;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=JCM19039_1474 {ECO:0000313|EMBL:GAK11759.1};
OS   Geomicrobium sp. JCM 19039.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX   NCBI_TaxID=1460636 {ECO:0000313|EMBL:GAK11759.1, ECO:0000313|Proteomes:UP000027177};
RN   [1] {ECO:0000313|EMBL:GAK11759.1, ECO:0000313|Proteomes:UP000027177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19039 {ECO:0000313|EMBL:GAK11759.1,
RC   ECO:0000313|Proteomes:UP000027177};
RA   Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA   Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA   Hongoh Y., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT   JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL   Genome Announc. 2:e00622-14(2014).
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   -!- 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:GAK11759.1}.
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DR   EMBL; BAXB01000005; GAK11759.1; -; Genomic_DNA.
DR   RefSeq; WP_042425284.1; NZ_BAXB01000005.1.
DR   AlphaFoldDB; A0A061P665; -.
DR   OrthoDB; 9792686at2; -.
DR   Proteomes; UP000027177; 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; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   PANTHER; PTHR40448; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR40448:SF1; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 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   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GAK11759.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027177};
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        171..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          328..517
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   522 AA;  58747 MW;  0A316267EB8EAD40 CRC64;
     MKKMKIRTRM LLFFTLLSSF LFIIFIIAFA SIEVDNTRSE YEQLARQTAN TIGYMPAIAD
     AVAIQDQEEL EGHIDRIRLQ VQQPIVSVVD DEKNVVYHSL DLNAQLSPSD EVYDRTIMFG
     SYQNNSELDE MSIQIIAPVY QQMADNGERL VGAVSVEYPR ETLMSSIADK FIRLGIVALI
     SLAVLGTGVV LFARNIREDT LGMEPVEIAS KFTERQAMLE SVKEGILAIN TDKKITLINP
     SARLLLHHEE DKILLIEALG LHDVIQKETF VYDEERTFNG YPLIANLRPM YTNKRLVGAI
     CSFRYKTDMR QLQLMMDQMK SYADGLRAQT HEFKNKLYVI MSLLQLEQYD EAIRFVQEEA
     IVTDQFLPKL NRIEDAGIQA ILLASMGKAA EKNIHMVIED RSSLSPTHIP ISSMTIMLGN
     VIDNAIEAVQ DEKQKNIGIF MTDIGDDIII EIEDSGVGIA RDEQHLVVEQ GYSRKGSGRG
     YGLYNVESTL REYNGSLEIA NSELGGACVS IILPKKERGI GS
//
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