ID   RSSA_SERMA              Reviewed;         469 AA.
AC   Q8GP19;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Swarming motility regulation sensor protein RssA;
DE            EC=2.7.13.3;
GN   Name=rssA;
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 HIS-248, MUTAGENESIS OF
RP   HIS-248, 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       {ECO:0000269|PubMed:15866926}.
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 {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
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; AAN28325.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GP19; -.
DR   SMR; Q8GP19; -.
DR   STRING; 273526.SMDB11_3307; -.
DR   iPTMnet; Q8GP19; -.
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; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..469
FT                   /note="Swarming motility regulation sensor protein RssA"
FT                   /id="PRO_0000074865"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          245..459
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         248
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT                   ECO:0000269|PubMed:16077114"
FT   MUTAGEN         248
FT                   /note="H->A: No autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:16077114"
SQ   SEQUENCE   469 AA;  52830 MW;  C1D7970BF008CF45 CRC64;
     MIGFKSFFMR TIIFQVLAIL LLWGLLVAWV KYWYYPDMEK YFDNQQRIVA AGIANILDET
     GTDNIDYRGI IKTIEGMYID SINNGMQDEI DYHPLFVVYD RDNRVLYSSQ TQGEPLRLPP
     SVLSGSVNYA GANWHLAGSW KEKRQYRVIV GESFNDRTTL FGNPADVPLL GILAAIIVTL
     LFTAYFSLRP LRQIARTISD RQPGNLSPIN VSEQYQEIRP VVMEVNKLMA RIDAANQREK
     RFMADAAHEL RTPIAAVLAQ LHLLTQVTEQ QERREIIGDM QQGLDRAASL SRQLINLAKL
     EAEDFPLKIE AVDIYAEIGK CIAQHVPYAL EKDVELSLDG SEDVVVSTDR RALIAIFTNL
     LDNALKYAPP GSRIEANIRS LAPLGCYITL RDNGPGVSEE HRSRLFERFY RVPGTQQTGS
     GLGLAIARNL ADKIGAQLRV TEGLDDRGIG FIIDLPESYR PQTESEPRP