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Database: UniProt
Entry: A0A097R3Z9_HAFAL
LinkDB: A0A097R3Z9_HAFAL
Original site: A0A097R3Z9_HAFAL 
ID   A0A097R3Z9_HAFAL        Unreviewed;       216 AA.
AC   A0A097R3Z9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Transcriptional regulatory protein RcsB {ECO:0000256|HAMAP-Rule:MF_00981};
GN   Name=rcsB {ECO:0000256|HAMAP-Rule:MF_00981};
GN   ORFNames=AT03_14325 {ECO:0000313|EMBL:AIU73445.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU73445.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU73445.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU73445.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog. 6:29-29(2014).
CC   -!- FUNCTION: Component of the Rcs signaling system, which controls
CC       transcription of numerous genes. RcsB is the response regulator that
CC       binds to regulatory DNA regions. {ECO:0000256|HAMAP-Rule:MF_00981}.
CC   -!- SUBUNIT: Interacts with RcsD. {ECO:0000256|HAMAP-Rule:MF_00981}.
CC   -!- PTM: Phosphorylated and activated by RcsD. {ECO:0000256|HAMAP-
CC       Rule:MF_00981}.
CC   -!- SIMILARITY: Belongs to the RcsB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00981}.
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DR   EMBL; CP009706; AIU73445.1; -; Genomic_DNA.
DR   RefSeq; WP_025798039.1; NZ_CP009706.1.
DR   AlphaFoldDB; A0A097R3Z9; -.
DR   GeneID; 78451594; -.
DR   KEGG; hav:AT03_14325; -.
DR   PATRIC; fig|1453496.5.peg.2923; -.
DR   eggNOG; COG2197; Bacteria.
DR   HOGENOM; CLU_000445_90_1_6; -.
DR   OrthoDB; 4313922at2; -.
DR   Proteomes; UP000029986; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   CDD; cd17535; REC_NarL-like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_00981; RcsB; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR030864; RcsB.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR45566; HTH-TYPE TRANSCRIPTIONAL REGULATOR YHJB-RELATED; 1.
DR   PANTHER; PTHR45566:SF2; NARL SUBFAMILY; 1.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS00622; HTH_LUXR_1; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00981};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00981, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000029986};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00981};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00981};
KW   Two-component regulatory system {ECO:0000256|HAMAP-Rule:MF_00981}.
FT   DOMAIN          5..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          144..209
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50043"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00981,
FT                   ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   216 AA;  23688 MW;  A83A477B286AE244 CRC64;
     MNNLNVIIAD DHPIVLFGIR KSLEQIEWVN VVGEFEDSTA LINSLSKLDA NVLITDLSMP
     GDKYGDGITL IKYIKRHYPH LSIIVLTMNN NPAILSAVLE LDIEGIVLKQ GAPADLPKAL
     AALQKGKKFT PESVSKLLEK ISASGYGDKR LSPKESEVLR LFAEGFLVTE IAKKLNRSIK
     TISSQKKSAM LKLGVDNDIA LLNYLSSVNI MSVDKD
//
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