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Database: UniProt
Entry: A0A259UWL3_9FIRM
LinkDB: A0A259UWL3_9FIRM
Original site: A0A259UWL3_9FIRM 
ID   A0A259UWL3_9FIRM        Unreviewed;       509 AA.
AC   A0A259UWL3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=phoR_4 {ECO:0000313|EMBL:OZC22402.1};
GN   ORFNames=SPACI_14510 {ECO:0000313|EMBL:OZC22402.1};
OS   Sporomusa acidovorans DSM 3132.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa.
OX   NCBI_TaxID=1123286 {ECO:0000313|EMBL:OZC22402.1, ECO:0000313|Proteomes:UP000216052};
RN   [1] {ECO:0000313|EMBL:OZC22402.1, ECO:0000313|Proteomes:UP000216052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3132 {ECO:0000313|EMBL:OZC22402.1,
RC   ECO:0000313|Proteomes:UP000216052};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Sporomusa acidovorans DSM 3132.";
RL   Submitted (FEB-2016) 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   -!- 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:OZC22402.1}.
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DR   EMBL; LSLL01000040; OZC22402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259UWL3; -.
DR   STRING; 112900.SAMN04488499_101475; -.
DR   Proteomes; UP000216052; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 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; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45453:SF3; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OZC22402.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          205..257
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          286..502
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          245..276
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   509 AA;  57299 MW;  49AA86CAFAD8942B CRC64;
     MTSVRTKLFL ILSGLVLFFV LISLASLGLG LKKFYVWQKQ DLLITTSRSI DQKYRGEPEE
     LSLELERAAN TLGAHISIFT PEGNIKYSSI SHILNKKQIE SPEPLPDVTP TPSPPSQFRI
     PPNSLQLIKS SQIIDSRTVV EMQLDQMLRI DFMVLKRQLQ SGDVLIIRQP LAPIAESAVA
     AAQFMSLTGL LTLLAGCVGA FFFSKRFTQP ILELKQIAQS MAKLDFSQKC KVNRDDELGE
     LGNSINHLSD QLDTAISALN QKNQQLLADV EKERALDKMR KSFVSNVSHE LKTPLSLILG
     YAEGLKENVV QDKESKDFYC SVIIDEAEKM DKLVKDLLNL SQLESGLFAL SRTDFDFCLL
     LRDIKKKYLS VLDEKLISLE INLPASQWVN GDPRRIEQVL LNLFTNALNY VKGSKHIKIW
     LEDTGKLIRF FIYNTGQPIP EDSLEKIWTS FYKTDEARTR ENGGYGLGLS IVRAIQEQHG
     NGYGVRNTAD GVIFWFDLNK AFPPVTPPS
//
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