GenomeNet

Database: UniProt
Entry: A0A3A9K460_9BACI
LinkDB: A0A3A9K460_9BACI
Original site: A0A3A9K460_9BACI 
ID   A0A3A9K460_9BACI        Unreviewed;      1104 AA.
AC   A0A3A9K460;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, 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   ORFNames=CR203_11495 {ECO:0000313|EMBL:RKL67129.1};
OS   Salipaludibacillus neizhouensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX   NCBI_TaxID=885475 {ECO:0000313|EMBL:RKL67129.1, ECO:0000313|Proteomes:UP000281498};
RN   [1] {ECO:0000313|EMBL:RKL67129.1, ECO:0000313|Proteomes:UP000281498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13187 {ECO:0000313|EMBL:RKL67129.1,
RC   ECO:0000313|Proteomes:UP000281498};
RA   Wang H.;
RT   "Bacillus sp. nov., a halophilic bacterium isolated from a Keqin Lake.";
RL   Submitted (OCT-2017) 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:RKL67129.1}.
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; PDOE01000004; RKL67129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9K460; -.
DR   OrthoDB; 9809348at2; -.
DR   Proteomes; UP000281498; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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; cd00075; HATPase; 1.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 2.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 2.
DR   Gene3D; 2.60.40.2380; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
DR   InterPro; IPR011006; CheY-like_superfamily.
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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF07696; 7TMR-DISMED2; 1.
DR   Pfam; PF02518; HATPase_c; 2.
DR   Pfam; PF00512; HisKA; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 2.
DR   SMART; SM00388; HisKA; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR   PROSITE; PS50109; HIS_KIN; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000281498};
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        188..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        217..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        285..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        342..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          429..647
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          686..803
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          871..1103
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          391..419
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          816..850
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         736
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1104 AA;  125702 MW;  34587514845CD8DE CRC64;
     MRIKTMKLPL LTLLFLFIFG IDVSATSVIT LDESSGSFRL DGLVEILEDK ENHWTFDDIQ
     TQELDEQFQP YHGVVPNFSY TSSVYWVKFQ LTNDSNENDW LLEIDNPTLD NVTLYSSESN
     LNFSRELTGD LLPFDMRDMD HRNFIFNLDL EPNHEKLIYL RFETQGAMQF PLTVYSPPSF
     LDKSELEYGI LGMFVGLGVV MAFYNLFLFF SLRNKSYLYY VIFIVANVFT HLAFTGLAYQ
     HIWSDAVWWN NRSIVFFMST SNIIAILFAK SFLEVKQNIP RLNRLLNVLV LFTVTVIIIL
     MVSYPTALNL SIVGIAITSI VIIAGAYMCL KKGFRPARYF LLAWIIFFGG VVISILADSG
     FIPVNFYTKY AWQLSSSLEL ILLSFALADK INTMRLEKEQ AKKNAIKSQK EMLESLQRND
     KLKDKFLAVT SHELRTPLNG IIGITASLQE GAAGDINDAM NSNLSMIKRS GTRLSHLIDD
     ILDFSKLENN NLDLSLKKVH LKEITDVVLT ICETLVRQKD IQLQNNIHSK IPAILADENR
     LQQILYNLIG NAIKYTEKGK VTIQAKEVNA KVIIEVIDTG IGIPKEYHES IFLPFNRGGN
     FTNNSYQGTG IGLNITKRLV ELQQGEISLE STTGKGSIFR FTLPTFKESS NVNSEIVSIE
     GSFSKERKEE PFREVHHVSF MNDGEKVLIA DDEPVNIQIL VNYLSLEGYN IQVVSDGEAV
     IQLIDQGAEF DMVMLDVMMP KLSGFEVCRL LRKQYSLTEL PILMLTAKNQ IEDRITAFEL
     GANDYLTKPV DKRELLSRTR TLINLRKSSI EAKERAQELD LLNQELIQMN DHLEEEVSSR
     TKELEFKNEE LDMRNMELIR VEKSRVALLS NISHELGTPL TFLQGYIQTV QEGYVNINDP
     KYLVLAQEKI KLLDRLIADI YDLSKFESGK MQLSMSPANA KEWFFCIYEK FEFEVKQSGL
     VMEKPFLKTS SDDERETLFI DIERMDQVLA NLIYNAIKHT PKGGGISLSG ELILYSESED
     TRDFTPHMIV EVRDTGNGIP EEEIPHIFNR FFKGSSQNIS GAKGSGLGLA ITKEIIDYHK
     GEIWVESTNK QGTSLFFSLP VVLS
//
DBGET integrated database retrieval system