ID   EPSB_RALSL              Reviewed;         750 AA.
AC   Q45409;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 105.
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;
OS   Ralstonia solanacearum (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AW;
RX   PubMed=7476194; DOI=10.1111/j.1365-2958.1995.tb02323.x;
RA   Huang J., Schell M.;
RT   "Molecular characterization of the eps gene cluster of Pseudomonas
RT   solanacearum and its transcriptional regulation at a single promoter.";
RL   Mol. Microbiol. 16:977-989(1995).
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.
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; U17898; AAA91625.1; -; Genomic_DNA.
DR   PIR; S77636; S77636.
DR   AlphaFoldDB; Q45409; -.
DR   SMR; Q45409; -.
DR   STRING; 859657.RPSI07_mp1012; -.
DR   TCDB; 8.A.3.3.3; the cytoplasmic membrane-periplasmic auxiliary-1 (mpa1) protein with cytoplasmic (c) domain (mpa1-c or mpa1+c) family.
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   Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
KW   Virulence.
FT   CHAIN           1..750
FT                   /note="Putative tyrosine-protein kinase EpsB"
FT                   /id="PRO_0000212359"
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..750
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   750 AA;  82266 MW;  E1ADBECFF98E0C72 CRC64;
     MTQNLPQPPA VNAPENELDL VRYLDVLVAN RWLIAGIAAA VMLLGAAYAF LARPVYEADI
     MVQVEDNPNS AKSLLGDVSS LFDVKTDANA EIEILRSRMV VGKAVDNLHL YITAKPRYFP
     LIGAWISSRA TRLSEPGLFG LGGYVWGTES IDVDGFDVPE ALEGQPFKLI VLGNGRYRLE
     NKSLDAPIEG VVGEPLEAKQ SIGTIQLQVN NLTAKAGATF ELERDSRLKT MEMLQDKLKI
     AEKGKQSGII GASLDGTNPA LTAAIMNQIA TEYVAQNIKR KAEEAERSLV FLDGLLPQLK
     LELERAEMKY NEMRNLRGTF DLSEEGKAFL QESVTVETSL QELKQKRAEL LTRFTSSHPG
     VQAIDQQISV MSGKVNSMTR RLKSLPNIEQ DTVRLMRDVQ VDNELYVSLL NDMQQLKLVK
     AGKVGNVRLV DGAAVPEEPV KPKKLTVTPL AGVLGVVLGV MAAFVRNALF GGITDPQDIE
     EHTGLSVYAT VPLSDTQVDL SGQLTTRKRG QYLLARRVPD DPSIEALRSL RTALQFAMQD
     AGNNLVVLTG PTPGVGKSFV SANLAAVIAT GGKRVLLIDA DMRKGYLHQY FGKDRKPGLL
     DLLAGNRSIE QVVHREVVPG LDFIATGLFP HNPSELLLNP RMVELMDTFR SQYDLVLVDT
     PPVLAVADTA ILAARAGLVL LVTRFERSTL GEIRETIKQL QHANVDVRGV VFNALDPNTY
     RYGYGSRYGR YRYVQYGYTS NSKPPEAESA