ID   EPSB_RALSO              Reviewed;         751 AA.
AC   P58593;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Putative tyrosine-protein kinase EpsB;
DE            EC=2.7.10.-;
DE   AltName: Full=EPS I polysaccharide export protein EpsB;
GN   Name=epsB; OrderedLocusNames=RSp1018; ORFNames=RS02356;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
CC   -!- FUNCTION: Probably involved in polymerization and/or export of
CC       exopolysaccharide EPS I which functions as a virulence factor. May be
CC       involved in an ATP-dependent process in the pathway for EPS I
CC       production, possibly export of the trimeric repeat units across the
CC       inner membrane or their polymerization (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the etk/wzc family. {ECO:0000305}.
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DR   EMBL; AL646053; CAD18169.1; -; Genomic_DNA.
DR   RefSeq; WP_011004308.1; NC_003296.1.
DR   AlphaFoldDB; P58593; -.
DR   SMR; P58593; -.
DR   STRING; 267608.RSp1018; -.
DR   EnsemblBacteria; CAD18169; CAD18169; RSp1018.
DR   GeneID; 60503929; -.
DR   KEGG; rso:RSp1018; -.
DR   PATRIC; fig|267608.8.peg.4499; -.
DR   eggNOG; COG0489; Bacteria.
DR   eggNOG; COG3206; Bacteria.
DR   HOGENOM; CLU_009912_0_0_4; -.
DR   OMA; VYGPKHP; -.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR005700; EPS_ExoP-like.
DR   InterPro; IPR005702; EPS_synthesis.
DR   InterPro; IPR032807; GNVR.
DR   InterPro; IPR003856; LPS_length_determ_N_term.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13614; AAA_31; 1.
DR   Pfam; PF13807; GNVR; 1.
DR   Pfam; PF02706; Wzz; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01007; eps_fam; 1.
DR   TIGRFAMs; TIGR01005; eps_transp_fam; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane;
KW   Exopolysaccharide synthesis; Kinase; Membrane; Nucleotide-binding; Plasmid;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase; Virulence.
FT   CHAIN           1..751
FT                   /note="Putative tyrosine-protein kinase EpsB"
FT                   /id="PRO_0000212358"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..444
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        445..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        466..751
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   751 AA;  82176 MW;  0F4EA613168C1282 CRC64;
     MTQNLSQPPA VNAPESELDL VRYLDVLVAN RWLIAGIAAV VMLLGATYAF LARPVYEADV
     LVQVEDNPNS AKSLLGDVSS LFDVKTDANA EIEILRSRMV VGKAVDNLHL YITAKPHYFP
     LIGAWVASRA KQLSEPGLFG LGGYTWGTEL IDVDGFDVPE ALEGQPFKLT ALGNGRYRLE
     NKSLDTPIEG VVGEPLEAKQ SVGTIQLLVN TLAAKAGAAF ELQRDSRLKT LEMLQDKLKI
     SEKGKQSGII GASLEGKNPA LTAAIMNQIA TEYVAQNIKR KAEEAERSLV FLDGLLPQLK
     LQLERAEMKY NEMRNLRGTF DLSEEGKAFL QESVTTETSL QELKQKRAEL LTRFTASHPG
     VQAIDQQIAV MSGKVGAMTR RLKSLPNIEQ DTVRLMRDVQ VDNDLYVSLL NDMQQLKLVK
     AGKVGNVRLV DGAAVPEEPV KPKKLTVTAL AGVLGVVLGV VAAFVRNTLF GGITEPQDIE
     EHTGLSVYAT VPLSDVQIDL SSQLTTHKRG QYLLARRVPD DPSIESLRSL RTALQFAMQD
     SGNNLVVLTG PTPGVGKSFV SANLAAVIAT GGKRVLLVDA DMRKGYLHQY FGKDRKPGLL
     DLLAGDRSIE QVVHREVVPG LDFIATGLFP HNPSELLLNP RMVELMDTFR AQYDLVLIDT
     PPVLAVTDTA ILAARAGTVL MVTRFERSTL GEIRETIKQL QHANVEVRGV VFNALDPNTY
     RYGYGSRYGR YRYVQYGYTS KPSAEAEAES A