ID   RPPB_SYNY3              Reviewed;         454 AA.
AC   Q55932;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 145.
DE   RecName: Full=Sensor histidine kinase RppB {ECO:0000303|PubMed:10894737};
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:P73276};
DE   AltName: Full=Sensor histidine kinase of nickel resistance operon NrsS {ECO:0000303|PubMed:11849552};
GN   Name=rppB {ECO:0000303|PubMed:10894737};
GN   Synonyms=nrsS {ECO:0000303|PubMed:11849552};
GN   OrderedLocusNames=sll0798 {ECO:0000312|EMBL:BAA10697.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION IN PHOTOSYSTEM BALANCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=10894737; DOI=10.1128/jb.182.15.4268-4277.2000;
RA   Li H., Sherman L.A.;
RT   "A redox-responsive regulator of photosynthesis gene expression in the
RT   cyanobacterium Synechocystis sp. Strain PCC 6803.";
RL   J. Bacteriol. 182:4268-4277(2000).
RN   [3]
RP   FUNCTION IN NICKEL RESPONSE, SUBCELLULAR LOCATION, INDUCTION BY NI(2+),
RP   OPERON, DISRUPTION PHENOTYPE, AND POSSIBLE TOPOLOGY.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=11849552; DOI=10.1046/j.1365-2958.2002.02741.x;
RA   Lopez-Maury L., Garcia-Dominguez M., Florencio F.J., Reyes J.C.;
RT   "A two-component signal transduction system involved in nickel sensing in
RT   the cyanobacterium Synechocystis sp. PCC 6803.";
RL   Mol. Microbiol. 43:247-256(2002).
CC   -!- FUNCTION: Member of two-component regulatory system RppA/RppB, involved
CC       in the establishment of the appropriate stoichiometry between the 2
CC       photosystems. It senses changes in the plastoquinone (PQ) redox poise
CC       (PubMed:10894737). Another group shows this two-component pair, renamed
CC       NrsR/NrsS, controls the nickel-dependent expression of the nrsBACD
CC       operon; they suggest the photosystem-related activities seen earlier
CC       are due to the expression of NrsS (RppB) in the absence of its natural
CC       substrate NrsR (RppA) (PubMed:11849552). {ECO:0000269|PubMed:10894737,
CC       ECO:0000269|PubMed:11849552}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P73276};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:11849552}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Expression of the rrpa-rrpB (nrsR-nrsS) operon is induced 3-
CC       fold by Ni(2+) and less by Co(2+). Autoregulates its own expression.
CC       {ECO:0000269|PubMed:11849552}.
CC   -!- DISRUPTION PHENOTYPE: Little visible phenotype, except up-regulation of
CC       nblA, a phycobilisome degradation protein (PubMed:10894737). A double
CC       rppA-rppB (nrsR-nrsS) deletion is less tolerant to growth on Ni(2+), no
CC       longer expresses nrsB (slr0793, involved in Ni(2+) resistance) in
CC       response to Ni(2+). Loss of expression of this operon. There are no
CC       growth effects, no changes in pigment concentration, no changes in PSII
CC       or nblA transcript levels seen in the double mutant (PubMed:11849552).
CC       {ECO:0000269|PubMed:10894737, ECO:0000269|PubMed:11849552}.
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DR   EMBL; BA000022; BAA10697.1; -; Genomic_DNA.
DR   PIR; S77005; S77005.
DR   AlphaFoldDB; Q55932; -.
DR   SMR; Q55932; -.
DR   IntAct; Q55932; 9.
DR   STRING; 1148.1001816; -.
DR   PaxDb; Q55932; -.
DR   EnsemblBacteria; BAA10697; BAA10697; BAA10697.
DR   KEGG; syn:sll0798; -.
DR   eggNOG; COG5002; Bacteria.
DR   InParanoid; Q55932; -.
DR   OMA; SSWGYLQ; -.
DR   PhylomeDB; Q55932; -.
DR   Proteomes; UP000001425; Chromosome.
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: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   Cell inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..454
FT                   /note="Sensor histidine kinase RppB"
FT                   /id="PRO_0000453146"
FT   TOPO_DOM        1..13
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:11849552"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..186
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:11849552"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..454
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:11849552"
FT   DOMAIN          230..448
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         233
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   454 AA;  50466 MW;  F0AB55B5D561D1EE CRC64;
     MNTRRLFARS RLQLAFWYAL VMGGILTLLG LGVYRAIVQA NWMALEREVE SIAGTLHDSL
     EPMLPSNASP TGVLQKMLPD LCLVNQPCQV NPTLIERHTL GISDRSLYYI RLFDYQGNLL
     AFSPNQPASL SSIFNQETWQ TIHPPTGDRY RQFTTILHSA GNTDKSSWGY LQIGRSLAAF
     DAENKRILWI LGLSFPIALG LVAFSSWGLA GLAMRPIYQS YQQQQQFTAN AAHELRSPLA
     SLLATVEAVL RIDSSHSPEI NTMLHTVERQ GRRLSQLITD LLLLSRLEQE TTAEDWRLCC
     LNDLVSDLTE EFLELAIAAH IDLSSDLSSG EVYAWGNESQ LYRLVSNLIA NAIQYTTAGG
     RVDITLTSHE QMAIITVQDT GIGIAPDQQE HIFERFYRVN RDRSRKTGGT GLGLAIAQVI
     TVKHRGSLTV ESALGKGSLF TIQLPIFSVP IVHS