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Database: UniProt
Entry: G9A2U5_RHIFH
LinkDB: G9A2U5_RHIFH
Original site: G9A2U5_RHIFH 
ID   G9A2U5_RHIFH            Unreviewed;       465 AA.
AC   G9A2U5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=ragB {ECO:0000313|EMBL:CCE95219.1};
GN   OrderedLocusNames=SFHH103_00720 {ECO:0000313|EMBL:CCE95219.1};
OS   Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE95219.1, ECO:0000313|Proteomes:UP000007735};
RN   [1] {ECO:0000313|EMBL:CCE95219.1, ECO:0000313|Proteomes:UP000007735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH103 {ECO:0000313|EMBL:CCE95219.1,
RC   ECO:0000313|Proteomes:UP000007735};
RX   PubMed=22374952; DOI=10.1128/JB.06729-11;
RA   Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA   Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA   Vinardell J.M., Zehner S., Gottfert M.;
RT   "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL   J. Bacteriol. 194:1617-1618(2012).
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};
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DR   EMBL; HE616890; CCE95219.1; -; Genomic_DNA.
DR   RefSeq; WP_014327731.1; NC_016812.1.
DR   AlphaFoldDB; G9A2U5; -.
DR   STRING; 1117943.SFHH103_00720; -.
DR   KEGG; sfh:SFHH103_00720; -.
DR   PATRIC; fig|380.5.peg.771; -.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3850; Bacteria.
DR   HOGENOM; CLU_000445_89_6_5; -.
DR   Proteomes; UP000007735; Chromosome.
DR   GO; GO:0016020; C:membrane; 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:SF8; HISTIDINE KINASE; 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   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCE95219.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCE95219.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          186..239
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          247..464
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   465 AA;  50357 MW;  CBCD3BBE8D7AD36A CRC64;
     MSKFGVLFRT TAVRLSALYL VLFSLCAVFL VFYVTGMSER FLQQQTREAI AVEASQIEEI
     YERAGVNGLL RSLERRARQP GANLYVIAGP SGEILAGNVA GLEPGLLDDE GWTSEPFRYQ
     RFTDENRADN HVALAQVLVL DNGLRILVGR DLQEPEKFRV LVRQALVVAL GIMGLGALVI
     WFGIGRNALR RIDRMSEAST KIMGGDLSQR LPTSGSGDEF DRLSESLNAM LGRIEKLNEG
     LKQVSDNIAH DLKTPLTRLR NKAEAALASK EGGNQNGALE EIIGESDQLI RTFNALLMIS
     RVEAGSAVAE MSEVDLSGIV GDCAELYEPV AEENALRLEA DIQPGVVISG NRELIGQALG
     NLIDNAIKYA EGTENPLLRV EMKKSGGNVV LTVADHGPGV PDTMRGEVVK RFVRLDESRS
     KPGTGLGLSL VEAVMEMHHG SLHLSATEPD GRGLAVRMVF PAGAT
//
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