BASS_SALTY
ID BASS_SALTY Reviewed; 356 AA.
AC P36557;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sensor protein BasS;
DE EC=2.7.13.3;
GN Name=basS; Synonyms=parB, pmrB; OrderedLocusNames=STM4291;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=8391535; DOI=10.1128/jb.175.13.4154-4164.1993;
RA Roland K.L., Martin L.E., Esther C.R., Spitznagel J.K.;
RT "Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-
RT component regulatory system with a possible role in virulence.";
RL J. Bacteriol. 175:4154-4164(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, INDUCTION, AND AUTOPHOSPHORYLATION.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=10480935; DOI=10.1074/jbc.274.38.27185;
RA Woesten M.M.S.M., Groisman E.A.;
RT "Molecular characterization of the PmrA regulon.";
RL J. Biol. Chem. 274:27185-27190(1999).
CC -!- FUNCTION: Member of the two-component regulatory system BasS/BasR.
CC Autophosphorylates and activates BasR by phosphorylation. Plays a role
CC in the adaptation of the organism to the host environment, in
CC particular to neutrophils, and therefore it plays a role in virulence
CC as well. {ECO:0000269|PubMed:10480935}.
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:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: The eptA-basRS operon is positively autoregulated by BasR
CC under high iron or aluminum concentration conditions.
CC {ECO:0000269|PubMed:10480935}.
CC -!- PTM: Autophosphorylated.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L13395; AAA72366.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23115.1; -; Genomic_DNA.
DR PIR; C40656; C40656.
DR RefSeq; NP_463156.1; NC_003197.2.
DR RefSeq; WP_001212189.1; NC_003197.2.
DR AlphaFoldDB; P36557; -.
DR SMR; P36557; -.
DR STRING; 99287.STM4291; -.
DR PaxDb; P36557; -.
DR EnsemblBacteria; AAL23115; AAL23115; STM4291.
DR GeneID; 1255817; -.
DR KEGG; stm:STM4291; -.
DR PATRIC; fig|99287.12.peg.4513; -.
DR HOGENOM; CLU_000445_89_37_6; -.
DR OMA; QLISVFW; -.
DR PhylomeDB; P36557; -.
DR BioCyc; SENT99287:STM4291-MON; -.
DR BRENDA; 2.7.13.3; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
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; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 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; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system;
KW Virulence.
FT CHAIN 1..356
FT /note="Sensor protein BasS"
FT /id="PRO_0000074702"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..64
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 89..141
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 149..356
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 152
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 356 AA; 40262 MW; 953234B125727BBD CRC64;
MRFQRRAMTL RQRLMLTIGL ILLVFQLIST FWLWHESTEQ IQLFEQALRD NRNNDRHIMH
EIREAVASLI VPGVFMVSLT LLICYQAVRR ITRPLAELQK ELEARTADNL APIAIHSSTL
EIESVVSAIN QLVTRLTTTL DNERLFTADV AHELRTPLSG VRLHLELLSK THNVDVAPLI
ARLDQMMDSV SQLLQLARVG QSFSSGNYQE VKLLEDVILP SYDELNTMLE TRQQTLLLPE
SAADVVVRGD ATLLRMLLRN LVENAHRYSP EGTHITIHIS ADPDAIMAVE DEGPGIDESK
CGKLSEAFVR MDSRYGGIGL GLSIVSRITQ LHQGQFFLQN RTERTGTRAW VLLKKA
