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Database: UniProt
Entry: B6IV75_RHOCS
LinkDB: B6IV75_RHOCS
Original site: B6IV75_RHOCS 
ID   B6IV75_RHOCS            Unreviewed;       744 AA.
AC   B6IV75;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=pleC {ECO:0000313|EMBL:ACJ00199.1};
GN   OrderedLocusNames=RC1_2827 {ECO:0000313|EMBL:ACJ00199.1};
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684 {ECO:0000313|EMBL:ACJ00199.1, ECO:0000313|Proteomes:UP000001591};
RN   [1] {ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACJ00199.1, ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX   PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA   Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA   Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA   Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT   "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT   proteobacterium Rhodospirillum centenum.";
RL   BMC Genomics 11:325-325(2010).
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; CP000613; ACJ00199.1; -; Genomic_DNA.
DR   RefSeq; WP_012567979.1; NC_011420.2.
DR   AlphaFoldDB; B6IV75; -.
DR   STRING; 414684.RC1_2827; -.
DR   KEGG; rce:RC1_2827; -.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_373336_0_0_5; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000001591; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 4.
DR   SMART; SM00091; PAS; 3.
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); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001591};
KW   Transferase {ECO:0000313|EMBL:ACJ00199.1}.
FT   DOMAIN          1..69
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          189..240
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          241..307
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          309..361
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          436..488
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          506..725
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   744 AA;  81873 MW;  8A23787CFCFF628B CRC64;
     MNLSPFFNLS QDLLSIVRTD GTIVALSPAW ERELGWSVAE LVATDGLDLL HPDDRRAARD
     RLRLLAAGQS PQRFELRCRR KDGRYLWLSG QSALSAGDGR IYSVCRDVTE SKRTALHLLA
     VESHSRVGTW DLDLETGVLN WSPMTHRIHA TDPATHRPYL EEAGRFFPGE ALPALLGAVA
     DLHQGGGPVR LELPFLTADG RARWVLFSAA AEAHAGRPRH VYGTLEDITE KRQERLHLLA
     FKDIVERSND GIWVLGPDGR TQYANGRMAA IMGCSEQDLL PARFLDHVLA EPRPRVADLL
     TGIVRVERDW SDFQMWRMDG SAFWASASIH PRRAPDGTLH STVVLVRDIS AWRRVELERE
     VNRARLELSQ NIARLGYWEL DLRSGSVFWS DVVYDIFGVS KDQGAHEQPA FLAAVHPDDR
     DRVLQMQQRI ESIGFADVEH RVVRPDGEVR WVHEVAKLDR DADGHPLRII GTVQDITPQK
     AVQARLDQAV AQAEAANRAK TQFLATMSHE LRTPLNAILG FSEIIRDGTF GQVSPGIYQE
     YAGHVFDSAS HLLDIINDVL DLAKVESATV TLTPEPVPLE ETVRRAVQTV RPIARDRRIS
     FAVQGGPAVT VLADRRALLQ SLYNILSNAL RHSPENGTVE VRLEPEDGFG ALTIRDFGPG
     FPPDVLAELG QPYPGRRNVY VSAARSTGLG YAITAALLGA MGGEIEACNA PDGGACVTFR
     LPLAPAPGAG AQVSDPVTAP APTA
//
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