NTRB_RHOCB
ID NTRB_RHOCB Reviewed; 355 AA.
AC P09431; D5AUA3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Sensory histidine kinase/phosphatase NtrB {ECO:0000250|UniProtKB:P0AFB5};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P0AFB5};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:P0AFB5};
DE AltName: Full=Nitrogen regulation protein NR(II) {ECO:0000250|UniProtKB:P0AFB5};
DE AltName: Full=Nitrogen regulator II {ECO:0000250|UniProtKB:P0AFB5};
DE Short=NRII {ECO:0000250|UniProtKB:P0AFB5};
GN Name=ntrB; Synonyms=nifR2; OrderedLocusNames=RCAP_rcc01797;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2710108; DOI=10.1007/bf00427050;
RA Jones R., Haselkorn R.;
RT "The DNA sequence of the Rhodobacter capsulatus ntrA, ntrB and ntrC gene
RT analogues required for nitrogen fixation.";
RL Mol. Gen. Genet. 215:507-516(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8355615; DOI=10.1111/j.1365-2958.1993.tb01636.x;
RA Foster-Hartnett D., Cullen P.J., Gabbert K.K., Kranz R.G.;
RT "Sequence, genetic, and lacZ fusion analyses of a nifR3-ntrB-ntrC operon in
RT Rhodobacter capsulatus.";
RL Mol. Microbiol. 8:903-914(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
CC -!- FUNCTION: Member of the two-component regulatory system NtrB/NtrC,
CC which controls expression of the nitrogen-regulated (ntr) genes in
CC response to nitrogen limitation. Under conditions of nitrogen
CC limitation, NtrB autophosphorylates and transfers the phosphoryl group
CC to NtrC. In the presence of nitrogen, acts as a phosphatase that
CC dephosphorylates and inactivates NtrC. {ECO:0000250|UniProtKB:P0AFB5}.
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:P0AFB5};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AFB5}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P0AFB5}.
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DR EMBL; X12359; CAA30921.1; -; Genomic_DNA.
DR EMBL; X72382; CAA51074.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85542.1; -; Genomic_DNA.
DR PIR; S03320; S03320.
DR RefSeq; WP_013067521.1; NC_014034.1.
DR AlphaFoldDB; P09431; -.
DR SMR; P09431; -.
DR IntAct; P09431; 1.
DR STRING; 272942.RCAP_rcc01797; -.
DR EnsemblBacteria; ADE85542; ADE85542; RCAP_rcc01797.
DR GeneID; 31490672; -.
DR KEGG; rcp:RCAP_rcc01797; -.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_39_5; -.
DR OMA; HGGRIDC; -.
DR OrthoDB; 1755994at2; -.
DR BRENDA; 2.7.13.3; 5381.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_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 SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Kinase; Nitrogen fixation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..355
FT /note="Sensory histidine kinase/phosphatase NtrB"
FT /id="PRO_0000074832"
FT DOMAIN 4..71
FT /note="PAS"
FT DOMAIN 136..352
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 139
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 130
FT /note="A -> AG (in Ref. 1; CAA30921 and 2; CAA51074)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="L -> V (in Ref. 1; CAA30921 and 2; CAA51074)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..282
FT /note="QRL -> SAV (in Ref. 1; CAA30921 and 2; CAA51074)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 38309 MW; B3EE3FED0B6C645F CRC64;
MNLPPPGIIW NSLPLPALML DVNDRVIEIN PAAELFLNLS ARALKGQALG ERLAISAPLE
EIFARVRKNR SALFVNDVDL TTGERAPVQC NLQAAPIADD PETVLLLISP REIADRLGRA
SMVKSAARSA IGMAEMLAHE IKNPLAGIAG AAQLLSMGLS GEDLELTDLI VDETRRIVKL
LEQVEQFGNV RPPEMKPVNI HDVLDRARKS AGVGFGAHML IVEDYDPSLP PTLGDADQLT
QVFLNLLKNA SEAAKGQGTI RLRTFYDYAL RLRRPDGGGQ RLPLQVEVID DGPGIPADIA
SSIFEPFVSG RENGTGLGLA LVSKIISEHN GWISVESAPG RTLFRISLPV APKEL
