REGB_CERS4
ID REGB_CERS4 Reviewed; 462 AA.
AC Q3J6C1; Q53068; Q53070;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Sensor histidine kinase RegB;
DE EC=2.7.13.3;
DE AltName: Full=Protein PrrB;
GN Name=regB; Synonyms=prrB; OrderedLocusNames=RHOS4_00950; ORFNames=RSP_1520;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7751278; DOI=10.1128/jb.177.10.2695-2706.1995;
RA Eraso J.M., Kaplan S.;
RT "Oxygen-insensitive synthesis of the photosynthetic membranes of
RT Rhodobacter sphaeroides: a mutant histidine kinase.";
RL J. Bacteriol. 177:2695-2706(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=10358089; DOI=10.1074/jbc.274.24.17290;
RA Ouchane S., Kaplan S.;
RT "Topological analysis of the membrane-localized redox-responsive sensor
RT kinase PrrB from Rhodobacter sphaeroides 2.4.1.";
RL J. Biol. Chem. 274:17290-17296(1999).
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:7751278}.
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
CC {ECO:0000269|PubMed:10358089}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10358089}.
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DR EMBL; U22347; AAA86723.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA77663.1; -; Genomic_DNA.
DR RefSeq; WP_002722232.1; NZ_CP030271.1.
DR RefSeq; YP_351564.1; NC_007493.2.
DR AlphaFoldDB; Q3J6C1; -.
DR SMR; Q3J6C1; -.
DR IntAct; Q3J6C1; 1.
DR MINT; Q3J6C1; -.
DR STRING; 272943.RSP_1520; -.
DR EnsemblBacteria; ABA77663; ABA77663; RSP_1520.
DR GeneID; 57468867; -.
DR GeneID; 67448285; -.
DR KEGG; rsp:RSP_1520; -.
DR PATRIC; fig|272943.9.peg.393; -.
DR eggNOG; COG2205; Bacteria.
DR OMA; LNRWHLM; -.
DR PhylomeDB; Q3J6C1; -.
DR BRENDA; 2.7.13.3; 5383.
DR Proteomes; UP000002703; Chromosome 1.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..462
FT /note="Sensor histidine kinase RegB"
FT /id="PRO_0000074860"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10358089"
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 46..51
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:10358089"
FT TRANSMEM 52..70
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 71..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10358089"
FT TRANSMEM 79..96
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 97..103
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:10358089"
FT TRANSMEM 104..123
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 124..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10358089"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 150..164
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:10358089"
FT TRANSMEM 165..182
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 183..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10358089"
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; 51033 MW; 3BC7CEA8C7BA7D5E CRC64;
MILGPDGILN RDTRGDWVRL RTLILLRWMA VAGQLAAIVV TDWYLGVRLP MGLCFMAVGA
SVIANVIATF VFPQNRRLTE FQALMILLFD LTQLSFLLFL TGGLTNPFAL LILAPVTISA
LALELRTTVI LGAIAIGLLT FTAYFHLPLI LADGSSLSVP RMFEFGFWLA IVIGILFLGL
YSRRVAIEIR SMSDALLATQ MALDREQKLT DLGGVVAAAA HELGTPLATI KLVSSELAEE
LSEQPALRDD AELIREQADR CRDILRSMGR AGKDDLQMRQ APLGEVLREA AEPHVGRGKR
VEFDLYPSRG GDERQPVILR RPEVIHGLRN LIQNAVDFAR STVWIDGEWT GDRIAIRIVD
DGEGYPPAII GRIGDPFVRQ RRAEESQSRR PGYEGMGLGL FIAKTLLERS GAELSFANAA
DPFLRSHERP ERCGAIVEVI WPVDRLVVVR NAPLGENVLI QT
