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Database: UniProt
Entry: A0A0U2L5C9_9BACL
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ID   A0A0U2L5C9_9BACL        Unreviewed;       496 AA.
AC   A0A0U2L5C9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=IJ22_49240 {ECO:0000313|EMBL:ALS25186.1}, SAMN05421868_105120
GN   {ECO:0000313|EMBL:SDI33303.1};
OS   Paenibacillus naphthalenovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS25186.1, ECO:0000313|Proteomes:UP000061660};
RN   [1] {ECO:0000313|Proteomes:UP000061660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA   Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT   "Complete genome sequences of two moderately thermophilic Paenibacillus
RT   species.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALS25186.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=32O-Y {ECO:0000313|EMBL:ALS25186.1};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ALS25186.1, ECO:0000313|Proteomes:UP000061660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-Y {ECO:0000313|EMBL:ALS25186.1,
RC   ECO:0000313|Proteomes:UP000061660};
RX   PubMed=26868401;
RA   Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT   "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT   Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL   Genome Announc. 4:e01717-15(2016).
RN   [4] {ECO:0000313|EMBL:SDI33303.1, ECO:0000313|Proteomes:UP000182184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR-N1 {ECO:0000313|EMBL:SDI33303.1,
RC   ECO:0000313|Proteomes:UP000182184};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP013652; ALS25186.1; -; Genomic_DNA.
DR   EMBL; FNDY01000005; SDI33303.1; -; Genomic_DNA.
DR   RefSeq; WP_054817334.1; NZ_FNDY01000005.1.
DR   AlphaFoldDB; A0A0U2L5C9; -.
DR   STRING; 162209.IJ22_49240; -.
DR   KEGG; pnp:IJ22_49240; -.
DR   PATRIC; fig|162209.4.peg.5202; -.
DR   OrthoDB; 335833at2; -.
DR   Proteomes; UP000061660; Chromosome.
DR   Proteomes; UP000182184; 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   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 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; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ALS25186.1};
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:UP000061660};
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        191..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          214..267
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          282..496
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          68..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  55703 MW;  1F6106C5AC1CD398 CRC64;
     MIRKVLDPVK RVMAPRSLRF QLLTRSLFIL AALLLLIGAL QYVLMKDFLY RNQAETMVTQ
     LRTLPRDILT RPNPLPERSS GDRAPGSQSD TGRPRGPVLF LPDMSVAYIG HDGTFIDLTR
     DNGSVSPRLS DEEYRSIQPS DHRGRVHYRV VRDEEGKEQL IVFRPVGLQI GGMFQMGTAT
     APLQDVVMRQ LLTFVALSVL ALAGGLAFYL PVLRRTLNPL DMMVKAVERT DAGNLAERFP
     GPQGQLEIDR LADSFNGMLE RLETSFEAER EAKEQMRRFI ADASHELRTP LTSIHGFLEV
     LLRGAADRPE QLYPALKSMH GESKRIKKLV EDLLMLAKLD RSPELQLKET RLDELIREME
     PHLRMLAGSR TVDFDLTAGI RGIYDSDKIK QVILNLFHNA VQHTDPEHGV IKVSLSSRRN
     QADLMIRDNG IGIAEEHIPH IFERFYRSDA SRTRKHGGAG LGLSISKSIV EAHDGTISVD
     SRPGKGCTFS VRLPAL
//
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