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RSSB_SERMA
ID   RSSB_SERMA              Reviewed;         219 AA.
AC   Q8GP20;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Swarming motility regulation protein RssB;
GN   Name=rssB;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=CH10;
RX   PubMed=15866926; DOI=10.1128/jb.187.10.3407-3414.2005;
RA   Lai H.-C., Soo P.-C., Wei J.-R., Yi W.-C., Liaw S.-J., Horng Y.-T.,
RA   Lin S.-M., Ho S.-W., Swift S., Williams P.;
RT   "The RssAB two-component signal transduction system in Serratia marcescens
RT   regulates swarming motility and cell envelope architecture in response to
RT   exogenous saturated fatty acids.";
RL   J. Bacteriol. 187:3407-3414(2005).
RN   [2]
RP   PROMOTER BINDING STUDIES, PHOSPHORYLATION AT ASP-51, MUTAGENESIS OF ASP-51,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=CH1;
RX   PubMed=16077114; DOI=10.1128/jb.187.16.5683-5690.2005;
RA   Wei J.-R., Tsai Y.-H., Soo P.-C., Horng Y.-T., Hsieh S.-C., Ho S.-W.,
RA   Lai H.-C.;
RT   "Biochemical characterization of RssA-RssB, a two-component signal
RT   transduction system regulating swarming behavior in Serratia marcescens.";
RL   J. Bacteriol. 187:5683-5690(2005).
CC   -!- FUNCTION: Member of the two-component regulatory system RssA/RssB
CC       involved in regulation of swarming motility which has been shown to be
CC       inhibited by saturated fatty acids. RssA/RssB regulates cellular fatty
CC       acid composition, hemolysin production and cell surface topography.
CC       RssA/RssB negatively regulates the activity of SlhBA. It can also act
CC       as a negative regulator for the control of the swarming initiation.
CC       RssB binds its own promoter. {ECO:0000269|PubMed:15866926}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutation in either rssA or rssB confers a
CC       precocious-swarming phenotype on LB agar: swarming occurs at 37 degrees
CC       Celsius and is initiated at a lower cell density and more rapidly than
CC       the swarming of the parent strain at 30 degrees Celsius. Both mutants
CC       also exhibit increased hemolysin activity and altered cell surface
CC       topology. {ECO:0000269|PubMed:16077114}.
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DR   EMBL; AF465237; AAN28326.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GP20; -.
DR   SMR; Q8GP20; -.
DR   STRING; 273526.SMDB11_3306; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111; PTHR48111; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Phosphoprotein; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..219
FT                   /note="Swarming motility regulation protein RssB"
FT                   /id="PRO_0000081222"
FT   DOMAIN          2..116
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        124..218
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT   MOD_RES         51
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT                   ECO:0000269|PubMed:16077114"
FT   MUTAGEN         51
FT                   /note="D->E: No phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:16077114"
SQ   SEQUENCE   219 AA;  24453 MW;  09B370891A397E28 CRC64;
     MNILLVEDDL QLGKALCRAL ELAGFNLCWV RLIADAENKL SSGGFDLMLL DLTLPDGDGL
     QKLIAWRAAG QNIPIIILTA RDRIESLVNS LDSGANDFLA KPFALPELIS RVKAVNRRMA
     GFASQTWSLG ALYLDPVNHQ VMLDNELLML SKKEYHLLHE LMRCAGTVVR KAVLEQRLFG
     HGDSVESNSL EVHMHNLRRK IGKDRVITVR GIGYLLKKE
 
 
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