ID A0A161ZPR4_9BACI Unreviewed; 861 AA.
AC A0A161ZPR4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AZI98_17690 {ECO:0000313|EMBL:KZN94827.1};
OS Aeribacillus pallidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Aeribacillus.
OX NCBI_TaxID=33936 {ECO:0000313|EMBL:KZN94827.1, ECO:0000313|Proteomes:UP000076476};
RN [1] {ECO:0000313|EMBL:KZN94827.1, ECO:0000313|Proteomes:UP000076476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8m3 {ECO:0000313|EMBL:KZN94827.1,
RC ECO:0000313|Proteomes:UP000076476};
RA Poltaraus A.B., Nazina T.N., Tourova T.P., Malakho S.M., Korshunova A.V.,
RA Sokolova D.S.;
RT "Draft genome sequence of Aeribacillus pallidus 8m3 from petroleum
RT reservoir.";
RL Submitted (APR-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:KZN94827.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWBR01000075; KZN94827.1; -; Genomic_DNA.
DR RefSeq; WP_063389574.1; NZ_QURG01000008.1.
DR AlphaFoldDB; A0A161ZPR4; -.
DR STRING; 33936.AZI98_17690; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000076476; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 3.
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; IPR005330; MHYT_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF03707; MHYT; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50924; MHYT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076476};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 72..93
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 105..123
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 208..227
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT DOMAIN 5..194
FT /note="MHYT"
FT /evidence="ECO:0000259|PROSITE:PS50924"
FT DOMAIN 241..311
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 313..364
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 403..438
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 629..844
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 348..375
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 861 AA; 98687 MW; FF49298C56FBAE9A CRC64;
MEALFNWELV ISSVVMAIIA SFFSVHMIQN IQVSTEKDKW LYIMLGTIWV GLGIWSMQFI
DMLGDDLYLI ATYYTVYTLL SFLLGIIASF AAFSMKDKQK NVSNAAAISI VVGLSIFVIY
YIGIKSLKGN EYDGFYSVLS NLIAFVLAGA VIAFFHHNKR SQKLQMKAII IPSIVLGLGI
FIFQYTVMNE IKKAGLFIYE QIYSVSTLLA NQLLLSIIMI FMIFAFVQKE KNKLERKFET
TNLYYESLIS YNPYIVFIIN TDGMITNINP KGLEILKAKK EQMIHQSIFS FLPQDDAERV
KQKMNRLLEH NENEMEVSFK NSKGEWIPLL LTFVPMIVEG KNEGFFVIAK DMKELKQYQK
RLRKMQKDLM NTLERQQGMT FKFVKINDQF IHTLCAGELL YKLGYSPHEI IGKDLRDFLP
KEVAEGQLRA YQKAWNGEIV HFEGKLNGYD YLAVLSPVIE NGKVVEVIGS CVDITVRKEQ
EMKLNESNAL RRTIIDNLPI GIVVIDHEMK IIALNKTILK IFQINEPIKQ LIGKNITNYF
PAVGRKVEEN TGEVSKIFTP YKHFSDEVNI KNGKILKRSY FPFYMDGKLK GHLWTFEDIT
EQKKMENSII QAKEEAVKAN MAKSEFLSKM SHELRTPLNG ILGFSHLLEL DKSLTEQQQA
FVEEILKGGR HLLNLINEIL DLSRIETGKI KISNDEVQID SVICECIALM KPAANKKRIK
IIKSIDQCVD QMIHIDSLRL KQVILNLLDN AIKYNVEGGQ IHITCKCQNG FLVIHIIDTG
IGICEEELKK IYEPFYRIQH VQVEGTGLGL SLVKQLIELM NGEFGVVSKI GEGSDFWIKL
PMLNRETNHA VKKDLEHRQH H
//
