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Database: UniProt
Entry: F7QQ22_9BRAD
LinkDB: F7QQ22_9BRAD
Original site: F7QQ22_9BRAD 
ID   F7QQ22_9BRAD            Unreviewed;       564 AA.
AC   F7QQ22;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CSIRO_3527 {ECO:0000313|EMBL:EGP06799.1};
OS   Bradyrhizobiaceae bacterium SG-6C.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae.
OX   NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP06799.1, ECO:0000313|Proteomes:UP000003148};
RN   [1] {ECO:0000313|EMBL:EGP06799.1, ECO:0000313|Proteomes:UP000003148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-6C {ECO:0000313|EMBL:EGP06799.1,
RC   ECO:0000313|Proteomes:UP000003148};
RX   PubMed=21742875; DOI=10.1128/JB.05647-11;
RA   Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA   Pandey G.;
RT   "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT   Bradyrhizobiaceae Strain SG-6C.";
RL   J. Bacteriol. 193:5057-5057(2011).
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}.
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:EGP06799.1}.
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DR   EMBL; AFOF01000031; EGP06799.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7QQ22; -.
DR   STRING; 709797.CSIRO_3527; -.
DR   eggNOG; COG2770; Bacteria.
DR   eggNOG; COG3920; Bacteria.
DR   HOGENOM; CLU_023848_1_0_5; -.
DR   Proteomes; UP000003148; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd12914; PDC1_DGC_like; 1.
DR   CDD; cd12915; PDC2_DGC_like; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR   PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR   PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF07536; HWE_HK; 1.
DR   SMART; SM00911; HWE_HK; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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}.
FT   TRANSMEM        285..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          305..358
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
SQ   SEQUENCE   564 AA;  61191 MW;  ACD5A26C3FC82F7A CRC64;
     MPLRNAIRRL SLTHRLLALT LVASLPGLAA VSYGAFDLRN TRYAEARAQA LRNAEVVVSE
     VDQIFDGIQA AMRAVAETDE VSRLNSTACT DYVVRVRPSI APLTSLLVVG LDGNIRCFSE
     PSLASPNLAD RDYFREAIDS KKFAIGTFIA SKVSDRNIIP MALPIIRDGK VEGAIVAGLN
     VEWLGQQLQQ RGVQSGGAVL IADRNGIVVS REPDREKFVG RKLDESLGRI GGSQPGSAEI
     TGVDGVQRII GYVPASMTPF GLYVSSGISR SEALAPIDRA VRNSIALFAL GSAIAFLLAW
     LVGESIIRRP LMRMVATAEA WRRGHDAART GIVGRSDEIG VLGQTFDRLM DENAMREEQR
     ATAEERREIL VHELAHRVKN TLATVQSIAS LSFRHSQGPE ALRQFHERLQ ALVRGHDLLT
     RKNWQHAQLS EIAEAAIAPL QEERGHRFAI SGPPVDLPPT TAVPMAMVLH ELCTNAMKYG
     ALSNNDGRVT IGWTAQPGDA GTVVSLIWSE SGGPPVTPPE EDGFGTRLIA NLSRQLGGDC
     TFRYPPSGLV FHLSMVAPAF EPRD
//
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