ID   VANS_ENTFA              Reviewed;         447 AA.
AC   Q47745;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Sensor protein VanSB;
DE            EC=2.7.13.3;
DE   AltName: Full=Vancomycin B-type resistance protein VanSB;
DE   AltName: Full=Vancomycin histidine protein kinase;
GN   Name=vanSB; OrderedLocusNames=EF_2298;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=8631706; DOI=10.1128/jb.178.5.1302-1309.1996;
RA   Evers S., Courvalin P.;
RT   "Regulation of VanB-type vancomycin resistance gene expression by the
RT   VanS(B)-VanR(B) two-component regulatory system in Enterococcus faecalis
RT   V583.";
RL   J. Bacteriol. 178:1302-1309(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Member of the two-component regulatory system VanS/VanR.
CC       Activates the transcription of vanH, vanA and vanX in response to
CC       vancomycin which results in vancomycin resistance. VanS activates VanR
CC       by phosphorylation.
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 membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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; U35369; AAB05623.1; -; Genomic_DNA.
DR   EMBL; AE016830; AAO82025.1; -; Genomic_DNA.
DR   RefSeq; NP_815955.1; NC_004668.1.
DR   RefSeq; WP_002368696.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q47745; -.
DR   SMR; Q47745; -.
DR   STRING; 226185.EF_2298; -.
DR   EnsemblBacteria; AAO82025; AAO82025; EF_2298.
DR   KEGG; efa:EF2298; -.
DR   PATRIC; fig|226185.45.peg.1234; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; IFARQMT; -.
DR   BRENDA; 2.7.13.3; 2095.
DR   Proteomes; UP000001415; Chromosome.
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   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
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   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Cell membrane;
KW   Cell wall biogenesis/degradation; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..447
FT                   /note="Sensor protein VanSB"
FT                   /id="PRO_0000074892"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          157..208
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          230..445
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         233
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   447 AA;  50112 MW;  6471F8A63C7498A2 CRC64;
     MERKGIFIKV FSYTIIVLLL LVGVTATLFA QQFVSYFRAM EAQQTVKSYQ PLVELIQNSD
     RLDMQEVAGL FHYNNQSFEF YIEDKEGSVL YATPNADTSN SVRPDFLYVV HRDDNISIVA
     QSKAGVGLLY QGLTIRGIVM IAIMVVFSLL CAYIFARQMT TPIKALADSA NKMANLKEVP
     PPLERKDELG ALAHDMHSMY IRLKETIARL EDEIAREHEL EETQRYFFAA ASHELKTPIA
     AVSVLLEGML ENIGDYKDHS KYLRECIKMM DRQGKTISEI LELVSLNDGR IVPIAEPLDI
     GRTVAELLPD FQTLAEANNQ RFVTDIPAGQ IVLSDPKLIQ KALSNVILNA VQNTPQGGEV
     RIWSEPGAEK YRLSVLNMGV HIDDTALSKL FIPFYRIDQA RSRKSGRSGL GLAIVQKTLD
     AMSLQYALEN TSDGVLFWLD LPPTSTL