ID   VANS_ENTFC              Reviewed;         384 AA.
AC   Q06240;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Sensor protein VanS;
DE            EC=2.7.13.3;
DE   AltName: Full=Vancomycin histidine protein kinase;
DE   AltName: Full=Vancomycin resistance protein VanS;
GN   Name=vanS;
OS   Enterococcus faecium (Streptococcus faecium).
OG   Plasmid pIP816.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BM4147; TRANSPOSON=Tn1546;
RX   PubMed=8380148; DOI=10.1128/jb.175.1.117-127.1993;
RA   Arthur M., Molinas C., Depardieu F., Courvalin P.;
RT   "Characterization of Tn1546, a Tn3-related transposon conferring
RT   glycopeptide resistance by synthesis of depsipeptide peptidoglycan
RT   precursors in Enterococcus faecium BM4147.";
RL   J. Bacteriol. 175:117-127(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BM4147;
RX   PubMed=1556077; DOI=10.1128/jb.174.8.2582-2591.1992;
RA   Arthur M., Molinas C., Courvalin P.;
RT   "The VanS-VanR two-component regulatory system controls synthesis of
RT   depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147.";
RL   J. Bacteriol. 174:2582-2591(1992).
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}.
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DR   EMBL; M97297; AAA65954.1; -; Genomic_DNA.
DR   EMBL; M68910; AAA24788.1; -; Genomic_DNA.
DR   PIR; B41838; B41838.
DR   RefSeq; WP_002305818.1; NZ_WQKY01000109.1.
DR   RefSeq; YP_001019037.1; NC_008821.1.
DR   RefSeq; YP_001974798.1; NC_010980.1.
DR   RefSeq; YP_002128397.1; NC_011140.1.
DR   RefSeq; YP_004172618.1; NC_014959.1.
DR   RefSeq; YP_976079.1; NC_008768.1.
DR   AlphaFoldDB; Q06240; -.
DR   SMR; Q06240; -.
DR   BRENDA; 2.7.13.3; 2096.
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:0043433; P:negative regulation of DNA-binding transcription factor activity; IGI:CACAO.
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; 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   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Cell membrane;
KW   Cell wall biogenesis/degradation; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Plasmid; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..384
FT                   /note="Sensor protein VanS"
FT                   /id="PRO_0000074893"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          161..376
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         164
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   384 AA;  43916 MW;  D69099844F37C35A CRC64;
     MVIKLKNKKN DYSKLERKLY MYIVAIVVVA IVFVLYIRSM IRGKLGDWIL SILENKYDLN
     HLDAMKLYQY SIRNNIDIFI YVAIVISILI LCRVMLSKFA KYFDEINTGI DVLIQNEDKQ
     IELSAEMDVM EQKLNTLKRT LEKREQDAKL AEQRKNDVVM YLAHDIKTPL TSIIGYLSLL
     DEAPDMPVDQ KAKYVHITLD KAYRLEQLID EFFEITRYNL QTITLTKTHI DLYYMLVQMT
     DEFYPQLSAH GKQAVIHAPE DLTVSGDPDK LARVFNNILK NAAAYSEDNS IIDITAGLSG
     DVVSIEFKNT GSIPKDKLAA IFEKFYRLDN ARSSDTGGAG LGLAIAKEII VQHGGQIYAE
     SNDNYTTFRV ELPAMPDLVD KRRS