ID   REGB_CERSP              Reviewed;         462 AA.
AC   P0C0Z0; Q53068; Q53070;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Sensor histidine kinase RegB;
DE            EC=2.7.13.3;
DE   AltName: Full=Protein PrrB;
GN   Name=regB; Synonyms=prrB;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=HR;
RX   PubMed=8550404; DOI=10.1128/jb.178.1.12-18.1996;
RA   Qian Y., Tabita F.R.;
RT   "A global signal transduction system regulates aerobic and anaerobic CO2
RT   fixation in Rhodobacter sphaeroides.";
RL   J. Bacteriol. 178:12-18(1996).
CC   -!- FUNCTION: Member of the two-component regulatory system RegB/RegA.
CC       Involved in the positive regulation of photosynthesis gene expression
CC       in response to anaerobiosis. Also involved in positive regulation of
CC       the cbbI and cbbII Calvin cycle CO2 fixation operons, as well as in
CC       regulation of expression of genes involved in alternative CO2 fixation
CC       pathways. Phosphorylates RegA/PrrA. {ECO:0000269|PubMed:8550404}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
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DR   EMBL; U22925; AAA93222.1; -; Genomic_DNA.
DR   PIR; B57145; B57145.
DR   AlphaFoldDB; P0C0Z0; -.
DR   SMR; P0C0Z0; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Gene3D; 3.30.565.10; -; 1.
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   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..462
FT                   /note="Sensor histidine kinase RegB"
FT                   /id="PRO_0000074859"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        26..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        46..51
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        52..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        71..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        79..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        97..103
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        104..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        124..129
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        130..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        150..164
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        165..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        183..462
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          218..445
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         221
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   462 AA;  51008 MW;  60EC9D6E8534BA07 CRC64;
     MILGPDGILN RDTRGDWWRL RTLILLRWMA VAGQLAAIVV TDWYLGVRLP MGLCFMAVGA
     SVIANVIATF VFPQNRRLTE FQALMILLFD LTQLSFLLFL TGGLTNPFAL LILAPVTISG
     VALDVRTTVI LGAIAIGLLT FTAYFHLPLI LADGSSLSVP RMFEFGFWLA IVIGILFLGL
     YSRRVAIEIR SMSDALLATQ MALDREQKLT DLGGVVAAAA HELGTPLATI KLVSSELAEE
     LSEQPALRDD ADVIREQADR CRDILRSMGR AGKDDLQMRQ GPLGEVLREA AEPHVGRGKR
     VEFDLYPSRG GDERQPVILR RPEVIHGVRN LIQNAVDFAR STVWIDGEWT GDRIAIRIVD
     DGEGYPPAII GRIGDPFVRQ RRAEESQSRR PGYEGMGLGL FIAKTLLERS GAELSFANAA
     DPFLRSHERP ERCGAIVEVI WPVDRLVVVR NAPLGENVLI QT